메뉴 건너뛰기




Volumn 49, Issue , 2017, Pages 16-35

Potential applications of antimicrobial peptides and their mimics in combating caries and pulpal infections

Author keywords

Antimicrobial peptides; Biofilms; Immunomodulation; Peptide mimics

Indexed keywords

HYDRAULIC STRUCTURES; MICROORGANISMS; NETWORK SECURITY; PEPTIDES;

EID: 85008249118     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2016.11.026     Document Type: Review
Times cited : (113)

References (222)
  • 2
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: general overview and clinical implications in human health and disease
    • [2] Guaní-Guerra, E., Santos-Mendoza, T., Lugo-Reyes, S.O., Terán, L.M., Antimicrobial peptides: general overview and clinical implications in human health and disease. Clin. Immunol. 135 (2010), 1–11.
    • (2010) Clin. Immunol. , vol.135 , pp. 1-11
    • Guaní-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Terán, L.M.4
  • 3
    • 84865973489 scopus 로고    scopus 로고
    • Next generation of antimicrobial peptides as molecular targeted medicines
    • [3] Aoki, W., Kuroda, K., Ueda, M., Next generation of antimicrobial peptides as molecular targeted medicines. J. Biosci. Bioeng. 114 (2012), 365–370.
    • (2012) J. Biosci. Bioeng. , vol.114 , pp. 365-370
    • Aoki, W.1    Kuroda, K.2    Ueda, M.3
  • 4
    • 84869098810 scopus 로고    scopus 로고
    • Expression systems for heterologous production of antimicrobial peptides
    • [4] Parachin, N.S., Mulder, K.C., Viana, A.A., Dias, S.C., Franco, O.L., Expression systems for heterologous production of antimicrobial peptides. Peptides 38 (2012), 446–456.
    • (2012) Peptides , vol.38 , pp. 446-456
    • Parachin, N.S.1    Mulder, K.C.2    Viana, A.A.3    Dias, S.C.4    Franco, O.L.5
  • 6
    • 70350441472 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: antimicrobial peptides, the small yet big players in innate and adaptive immunity
    • [6] Auvynet, C., Rosenstein, Y., Multifunctional host defense peptides: antimicrobial peptides, the small yet big players in innate and adaptive immunity. FEBS. J. 276 (2009), 6497–6508.
    • (2009) FEBS. J. , vol.276 , pp. 6497-6508
    • Auvynet, C.1    Rosenstein, Y.2
  • 7
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense
    • [7] Lai, Y., Gallo, R.L., AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 30 (2009), 131–141.
    • (2009) Trends Immunol. , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 8
    • 77952791627 scopus 로고    scopus 로고
    • The role of salivary histatin and the human cathelicidin LL-37 in wound healing and innate immunity
    • [8] Oudhoff, M.J., Blaauboer, M.E., Nazmi, K., Scheres, N., Bolscher, J.G., Veerman, E.C., The role of salivary histatin and the human cathelicidin LL-37 in wound healing and innate immunity. Biol. Chem. 391 (2010), 541–548.
    • (2010) Biol. Chem. , vol.391 , pp. 541-548
    • Oudhoff, M.J.1    Blaauboer, M.E.2    Nazmi, K.3    Scheres, N.4    Bolscher, J.G.5    Veerman, E.C.6
  • 9
    • 79251599753 scopus 로고    scopus 로고
    • Host defense peptides and their antimicrobial-immunomodulatory duality
    • [9] Steinstraesser, L., Kraneburg, U., Jacobsen, F., Al-Benna, S., Host defense peptides and their antimicrobial-immunomodulatory duality. Immunobiology 216 (2011), 322–333.
    • (2011) Immunobiology , vol.216 , pp. 322-333
    • Steinstraesser, L.1    Kraneburg, U.2    Jacobsen, F.3    Al-Benna, S.4
  • 10
    • 84860601877 scopus 로고    scopus 로고
    • Antimicrobial peptides: key components of the innate immune system
    • [10] Pasupuleti, M., Schmidtchen, A., Malmsten, M., Antimicrobial peptides: key components of the innate immune system. Crit. Rev. Biotechnol. 32 (2012), 143–171.
    • (2012) Crit. Rev. Biotechnol. , vol.32 , pp. 143-171
    • Pasupuleti, M.1    Schmidtchen, A.2    Malmsten, M.3
  • 11
    • 84863331797 scopus 로고    scopus 로고
    • N, Cationic host defence peptides: multifaceted role in immune modulation and inflammation
    • [11] Choi, K.Y., Chow, L.N., Mookherjee, N., N, Cationic host defence peptides: multifaceted role in immune modulation and inflammation. J. Innate Immun. 4 (2012), 361–370.
    • (2012) J. Innate Immun. , vol.4 , pp. 361-370
    • Choi, K.Y.1    Chow, L.N.2    Mookherjee, N.3
  • 12
    • 0038492604 scopus 로고    scopus 로고
    • Starvation survival, growth and recovery of Enterococcus faecalis in human serum
    • [12] Figdor, D., Davies, J.K., Sundqvist, G., Starvation survival, growth and recovery of Enterococcus faecalis in human serum. Oral Microbiol. Immunol. 18 (2003), 234–239.
    • (2003) Oral Microbiol. Immunol. , vol.18 , pp. 234-239
    • Figdor, D.1    Davies, J.K.2    Sundqvist, G.3
  • 13
    • 84922778233 scopus 로고    scopus 로고
    • Antimicrobial peptide-based treatment for endodontic infections–biotechnological innovation in endodontics
    • [13] Lima, S.M., de Padua, G.M., Sousa, M.G., Freire Mde, S., Franco, O.L., Rezende, T.M., Antimicrobial peptide-based treatment for endodontic infections–biotechnological innovation in endodontics. Biotechnol. Adv. 33 (2015), 203–213.
    • (2015) Biotechnol. Adv. , vol.33 , pp. 203-213
    • Lima, S.M.1    de Padua, G.M.2    Sousa, M.G.3    Freire Mde, S.4    Franco, O.L.5    Rezende, T.M.6
  • 14
    • 84990217472 scopus 로고    scopus 로고
    • Identification of antimicrobial peptides by using eigenvectors
    • [Epub ahead of print]
    • [14] Polanco, C., Identification of antimicrobial peptides by using eigenvectors. Acta Biochim. Pol., 2016 [Epub ahead of print].
    • (2016) Acta Biochim. Pol.
    • Polanco, C.1
  • 15
    • 84979498105 scopus 로고    scopus 로고
    • APD3: the antimicrobial peptide database as a tool for research and education
    • [15] Wang, G., Li, X., Wang, Z., APD3: the antimicrobial peptide database as a tool for research and education. Nucleic Acids Res. 44 (2016), D1087–D1093.
    • (2016) Nucleic Acids Res. , vol.44 , pp. D1087-D1093
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 16
    • 84979519007 scopus 로고    scopus 로고
    • CAMPR3: a database on sequences, structures and signatures of antimicrobial peptides
    • [16] Waghu, F.H., Barai, R.S., Gurung, P., Idicula-Thomas, S., CAMPR3: a database on sequences, structures and signatures of antimicrobial peptides. Nucleic Acids Res. 44 (2016), D1094–D1097.
    • (2016) Nucleic Acids Res. , vol.44 , pp. D1094-D1097
    • Waghu, F.H.1    Barai, R.S.2    Gurung, P.3    Idicula-Thomas, S.4
  • 18
    • 29144521244 scopus 로고    scopus 로고
    • Human antimicrobial peptides: defensins, cathelicidins and histatins
    • [18] De Smet, K., Contreras, R., Human antimicrobial peptides: defensins, cathelicidins and histatins. Biotechnol. Lett. 27 (2005), 1337–1347.
    • (2005) Biotechnol. Lett. , vol.27 , pp. 1337-1347
    • De Smet, K.1    Contreras, R.2
  • 19
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • [19] Hancock, R.E., Sahl, H.G., Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24 (2006), 1551–1557.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 20
    • 84856864352 scopus 로고    scopus 로고
    • Antimicrobial peptides: old molecules with new ideas
    • [20] Nakatsuji, T., Gallo, R.L., Antimicrobial peptides: old molecules with new ideas. J. Invest. Dermatol. 132 (2012), 887–895.
    • (2012) J. Invest. Dermatol. , vol.132 , pp. 887-895
    • Nakatsuji, T.1    Gallo, R.L.2
  • 21
  • 22
    • 0036740432 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 is expressed by keratinocytes in condyloma acuminatum and verruca vulgaris
    • [22] Conner, K., Nern, K., Rudisill, J., O'Grady, T., Gallo, R.L., The antimicrobial peptide LL-37 is expressed by keratinocytes in condyloma acuminatum and verruca vulgaris. J. Am. Acad. Dermatol. 47 (2002), 347–350.
    • (2002) J. Am. Acad. Dermatol. , vol.47 , pp. 347-350
    • Conner, K.1    Nern, K.2    Rudisill, J.3    O'Grady, T.4    Gallo, R.L.5
  • 24
    • 84863757781 scopus 로고    scopus 로고
    • Role of defensins and cathelicidin LL37 in auto-immune and auto-inflammatory diseases
    • [24] Frasca, L., Lande, R., Role of defensins and cathelicidin LL37 in auto-immune and auto-inflammatory diseases. Curr. Pharm. Biotechnol. 13 (2012), 1882–1897.
    • (2012) Curr. Pharm. Biotechnol. , vol.13 , pp. 1882-1897
    • Frasca, L.1    Lande, R.2
  • 25
    • 84876768300 scopus 로고    scopus 로고
    • Chemical methods for peptide and protein production
    • [25] Chandrudu, S., Simerska, P., Toth, I., Chemical methods for peptide and protein production. Molecules 18 (2013), 4373–4388.
    • (2013) Molecules , vol.18 , pp. 4373-4388
    • Chandrudu, S.1    Simerska, P.2    Toth, I.3
  • 26
    • 84930333296 scopus 로고    scopus 로고
    • Antimicrobial peptides: their role as infection-selective tracers for molecular imaging
    • [26] Ebenhan, T., Gheysens, O., Kruger, H.G., Zeevaart, J.R., Sathekge, M.M., Antimicrobial peptides: their role as infection-selective tracers for molecular imaging. Biomed. Res. Int., 2014, 2014, 867381.
    • (2014) Biomed. Res. Int. , vol.2014 , pp. 867381
    • Ebenhan, T.1    Gheysens, O.2    Kruger, H.G.3    Zeevaart, J.R.4    Sathekge, M.M.5
  • 27
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • [27] Yeaman, M.R., Yount, N.Y., Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev. 55 (2003), 27–55.
    • (2003) Pharmacol Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 28
    • 44649154576 scopus 로고    scopus 로고
    • The pharmacology of radiolabeled cationic antimicrobial peptides
    • [28] Brouwer, C.P., Wulferink, M., Welling, M.M., The pharmacology of radiolabeled cationic antimicrobial peptides. J. Pharm. Sci. 97 (2008), 1633–1651.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 1633-1651
    • Brouwer, C.P.1    Wulferink, M.2    Welling, M.M.3
  • 29
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • [29] Epand, R.M., Vogel, H.J., Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462 (1999), 11–28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 30
    • 0035929565 scopus 로고    scopus 로고
    • Interaction of cationic antimicrobial peptides with model membranes
    • [30] Zhang, L., Rozek, A., Hancock, R.E., Interaction of cationic antimicrobial peptides with model membranes. J. Biol. Chem. 276 (2001), 35714–35722.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35714-35722
    • Zhang, L.1    Rozek, A.2    Hancock, R.E.3
  • 31
    • 77955846576 scopus 로고    scopus 로고
    • Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity
    • [31] Takahashi, D., Shukla, S.K., Prakash, O., Zhang, G., Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity. Biochimie 92 (2010), 1236–1241.
    • (2010) Biochimie , vol.92 , pp. 1236-1241
    • Takahashi, D.1    Shukla, S.K.2    Prakash, O.3    Zhang, G.4
  • 32
    • 0035719931 scopus 로고    scopus 로고
    • Amphipathic alpha helical antimicrobial peptides
    • [32] Giangaspero, A., Sandri, L., Tossi, A., Amphipathic alpha helical antimicrobial peptides. Eur. J. Biochem. 268 (2001), 5589–5600.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5589-5600
    • Giangaspero, A.1    Sandri, L.2    Tossi, A.3
  • 33
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells
    • [33] Dathe, M., Wieprecht, T., Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim. Biophys. Acta 1462 (1999), 71–87.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 34
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • [34] Brogden, K.A., Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol. 3 (2005), 238–250.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 35
    • 84856774559 scopus 로고    scopus 로고
    • Role of lipids in the interaction of antimicrobial peptides with membranes
    • [35] Teixeira, V., Feio, M.J., Bastos, M., Role of lipids in the interaction of antimicrobial peptides with membranes. Prog. Lipid Res. 51 (2012), 149–177.
    • (2012) Prog. Lipid Res. , vol.51 , pp. 149-177
    • Teixeira, V.1    Feio, M.J.2    Bastos, M.3
  • 36
    • 84947600267 scopus 로고
    • Gram-positive bacterial cell envelopes: The impact on the activity of antimicrobial peptides
    • [36] Malanovic, N., Lohner, K., Gram-positive bacterial cell envelopes: The impact on the activity of antimicrobial peptides. Biochim. Biophys. Acta. 2016 (1858), 936–946.
    • (1858) Biochim. Biophys. Acta. , vol.2016 , pp. 936-946
    • Malanovic, N.1    Lohner, K.2
  • 37
    • 84910615623 scopus 로고    scopus 로고
    • Antimicrobial GL13K peptide coatings killed and ruptured the wall of Streptococcus gordonii and prevented formation and growth of biofilms
    • [37] Chen, X., Hirt, H., Li, Y., Gorr, S.U., Aparicio, C., Antimicrobial GL13K peptide coatings killed and ruptured the wall of Streptococcus gordonii and prevented formation and growth of biofilms. PLoS ONE, 9, 2014, e111579.
    • (2014) PLoS ONE , vol.9 , pp. e111579
    • Chen, X.1    Hirt, H.2    Li, Y.3    Gorr, S.U.4    Aparicio, C.5
  • 38
    • 40949089662 scopus 로고    scopus 로고
    • Teichoic acids and related cell-wall glycopolymers in Gram- positive physiology and host interactions
    • [38] Weidenmaier, C., Peschel, A., Teichoic acids and related cell-wall glycopolymers in Gram- positive physiology and host interactions. Nature Rev. Microbiol. 6 (2008), 276–287.
    • (2008) Nature Rev. Microbiol. , vol.6 , pp. 276-287
    • Weidenmaier, C.1    Peschel, A.2
  • 39
    • 84908200723 scopus 로고    scopus 로고
    • Treatment of microbial biofilms in the post-antibiotic era: prophylactic and therapeutic use of antimicrobial peptides and their design by bioinformatics tools
    • [39] Di Luca, M., Maccari, G., Nifosì, R., Treatment of microbial biofilms in the post-antibiotic era: prophylactic and therapeutic use of antimicrobial peptides and their design by bioinformatics tools. Pathog. Dis. 70 (2014), 257–270.
    • (2014) Pathog. Dis. , vol.70 , pp. 257-270
    • Di Luca, M.1    Maccari, G.2    Nifosì, R.3
  • 40
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • [40] Zasloff, M., Antimicrobial peptides of multicellular organisms. Nature 415 (2002), 389–395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 41
    • 0036119654 scopus 로고    scopus 로고
    • Saliva - the defender of the oral cavity
    • [41] Amerongen, A.V., Veerman, E.C., Saliva - the defender of the oral cavity. Oral Dis. 8 (2002), 12–22.
    • (2002) Oral Dis. , vol.8 , pp. 12-22
    • Amerongen, A.V.1    Veerman, E.C.2
  • 42
    • 79951917226 scopus 로고    scopus 로고
    • Antimicrobial peptides and periodontal disease
    • [42] Gorr, S.U., Abdolhosseini, M., Antimicrobial peptides and periodontal disease. J. Clin. Periodontol. 38:Suppl 11 (2011), 126–141.
    • (2011) J. Clin. Periodontol. , vol.38 , pp. 126-141
    • Gorr, S.U.1    Abdolhosseini, M.2
  • 43
    • 41449087185 scopus 로고    scopus 로고
    • Host defense peptides in the oral cavity
    • [43] Devine, D.A., Cosseau, C., Host defense peptides in the oral cavity. Adv. Appl. Microbiol. 63 (2008), 281–322.
    • (2008) Adv. Appl. Microbiol. , vol.63 , pp. 281-322
    • Devine, D.A.1    Cosseau, C.2
  • 44
    • 36348997293 scopus 로고    scopus 로고
    • Oral antimicrobial peptides and biological control of caries
    • [44] Dale, B.A., Tao, R., Kimball, J.R., Jurevic, R.J., Oral antimicrobial peptides and biological control of caries. BMC Oral Health., 6(Suppl 1), 2006, S13.
    • (2006) BMC Oral Health. , vol.6 , pp. S13
    • Dale, B.A.1    Tao, R.2    Kimball, J.R.3    Jurevic, R.J.4
  • 46
    • 2542480000 scopus 로고    scopus 로고
    • Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
    • [46] Yang, D., Biragyn, A., Hoover, D.M., Lubkowski, J., Oppenheim, J.J., Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annu. Rev. Immunol. 22 (2004), 181–215.
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 181-215
    • Yang, D.1    Biragyn, A.2    Hoover, D.M.3    Lubkowski, J.4    Oppenheim, J.J.5
  • 47
    • 0026200199 scopus 로고
    • Bacteria in the apical 5 mm of infected root canals
    • [47] Baumgartner, J.C., Falkler, W.A. Jr, Bacteria in the apical 5 mm of infected root canals. J. Endod. 17 (1991), 380–383.
    • (1991) J. Endod. , vol.17 , pp. 380-383
    • Baumgartner, J.C.1    Falkler, W.A.2
  • 49
    • 0032321488 scopus 로고    scopus 로고
    • Periapical inflammatory responses and their modulation
    • [49] Stashenko, P., Teles, R., D'Souza, R., Periapical inflammatory responses and their modulation. Crit. Rev. Oral Biol. Med. 9 (1998), 498–521.
    • (1998) Crit. Rev. Oral Biol. Med. , vol.9 , pp. 498-521
    • Stashenko, P.1    Teles, R.2    D'Souza, R.3
  • 50
    • 0022400032 scopus 로고
    • Inflammatory and immunological aspects of the pathogenesis of human periapical lesions
    • [50] Torabinejad, M., Eby, W.C., Naidorf, I.J., Inflammatory and immunological aspects of the pathogenesis of human periapical lesions. J. Endod. 11 (1985), 479–488.
    • (1985) J. Endod. , vol.11 , pp. 479-488
    • Torabinejad, M.1    Eby, W.C.2    Naidorf, I.J.3
  • 51
    • 0033180667 scopus 로고    scopus 로고
    • Antibiotic resistance in the subgingival microflora in patients with adult periodontitis. A comparative survey between Spain and the Netherlands
    • [51] van Winkelhoff, A.J., Herrera, D., Winkel, E.G., Dellemijn-Kippuw, N., Vandenbroucke-Grauls, C.M., Sanz, M., Antibiotic resistance in the subgingival microflora in patients with adult periodontitis. A comparative survey between Spain and the Netherlands. Ned. Tijdschr. Tandheelkd. 106 (1999), 290–294.
    • (1999) Ned. Tijdschr. Tandheelkd. , vol.106 , pp. 290-294
    • van Winkelhoff, A.J.1    Herrera, D.2    Winkel, E.G.3    Dellemijn-Kippuw, N.4    Vandenbroucke-Grauls, C.M.5    Sanz, M.6
  • 52
    • 0842264381 scopus 로고    scopus 로고
    • Prevalence, proportions, and identities of antibiotic-resistant bacteria in the oral microflora of healthy children
    • [52] Ready, D., Bedi, R., Spratt, D.A., Mullany, P., Wilson, M., Prevalence, proportions, and identities of antibiotic-resistant bacteria in the oral microflora of healthy children. Microb. Drug. Resist. 9 (2003), 367–372.
    • (2003) Microb. Drug. Resist. , vol.9 , pp. 367-372
    • Ready, D.1    Bedi, R.2    Spratt, D.A.3    Mullany, P.4    Wilson, M.5
  • 53
    • 16544366411 scopus 로고    scopus 로고
    • Antibiotic resistance in general dental practice–a cause for concern?
    • [53] Sweeney, L.C., Dave, J., Chambers, P.A., Heritage, J., Antibiotic resistance in general dental practice–a cause for concern?. J. Antimicrob. Chemother. 53 (2004), 567–576.
    • (2004) J. Antimicrob. Chemother. , vol.53 , pp. 567-576
    • Sweeney, L.C.1    Dave, J.2    Chambers, P.A.3    Heritage, J.4
  • 54
    • 24644485249 scopus 로고    scopus 로고
    • The maintenance in the oral cavity of children of tetracycline-resistant bacteria and the genes encoding such resistance
    • [54] Lancaster, H., Bedi, R., Wilson, M., Mullany, P., The maintenance in the oral cavity of children of tetracycline-resistant bacteria and the genes encoding such resistance. J. Antimicrob. Chemother. 56 (2005), 524–531.
    • (2005) J. Antimicrob. Chemother. , vol.56 , pp. 524-531
    • Lancaster, H.1    Bedi, R.2    Wilson, M.3    Mullany, P.4
  • 55
    • 33646244246 scopus 로고    scopus 로고
    • Determining the antibiotic resistance potential of the indigenous oral microbiota of humans using a metagenomic approach
    • [55] Diaz-Torres, M.L., Villedieu, A., Hunt, N., McNab, R., Spratt, D.A., Allan, E., Mullany, P., Wilson, M., Determining the antibiotic resistance potential of the indigenous oral microbiota of humans using a metagenomic approach. FEMS Microbiol. Lett. 258 (2006), 257–262.
    • (2006) FEMS Microbiol. Lett. , vol.258 , pp. 257-262
    • Diaz-Torres, M.L.1    Villedieu, A.2    Hunt, N.3    McNab, R.4    Spratt, D.A.5    Allan, E.6    Mullany, P.7    Wilson, M.8
  • 56
    • 38349165316 scopus 로고    scopus 로고
    • Bacterial resistance and the dental professionals’ role to halt the problem
    • [56] Al-Haroni, M., Bacterial resistance and the dental professionals’ role to halt the problem. J. Dent. 36 (2008), 95–103.
    • (2008) J. Dent. , vol.36 , pp. 95-103
    • Al-Haroni, M.1
  • 57
    • 79959649508 scopus 로고    scopus 로고
    • Antibiotic resistance and adhesion properties of oral Enterococci associated to dental caries
    • [57] Kouidhi, B., Zmantar, T., Mahdouani, K., Hentati, H., Bakhrouf, A., Antibiotic resistance and adhesion properties of oral Enterococci associated to dental caries. BMC Microbiol., 11, 2011, 155.
    • (2011) BMC Microbiol. , vol.11 , pp. 155
    • Kouidhi, B.1    Zmantar, T.2    Mahdouani, K.3    Hentati, H.4    Bakhrouf, A.5
  • 58
    • 84864685407 scopus 로고    scopus 로고
    • Mechanisms of action of systemic antibiotics used in periodontal treatment and mechanisms of bacterial resistance to these drugs
    • [58] Soares, G.M., Figueiredo, L.C., Faveri, M., Cortelli, S.C., Duarte, P.M., Feres, M., Mechanisms of action of systemic antibiotics used in periodontal treatment and mechanisms of bacterial resistance to these drugs. J. Appl. Oral Sci. 20 (2012), 295–309.
    • (2012) J. Appl. Oral Sci. , vol.20 , pp. 295-309
    • Soares, G.M.1    Figueiredo, L.C.2    Faveri, M.3    Cortelli, S.C.4    Duarte, P.M.5    Feres, M.6
  • 59
    • 84928897740 scopus 로고    scopus 로고
    • Prevalence of antibiotic resistance genes in subjects with successful and failing dental implants. A pilot study, Open
    • [59] Koukos, G., Papadopoulos, C., Tsalikis, L., Sakellari, D., Arsenakis, M., Konstantinidis, A., Prevalence of antibiotic resistance genes in subjects with successful and failing dental implants. A pilot study, Open. Dent. J. 8 (2015), 257–263.
    • (2015) Dent. J. , vol.8 , pp. 257-263
    • Koukos, G.1    Papadopoulos, C.2    Tsalikis, L.3    Sakellari, D.4    Arsenakis, M.5    Konstantinidis, A.6
  • 60
    • 84971643922 scopus 로고    scopus 로고
    • Prevalence of β-lactam (bla TEM) and metronidazole (nim) resistance genes in the oral cavity of Greek subjects
    • [60] Koukos, G., Konstantinidis, A., Tsalikis, L., Arsenakis, M., Slini, T., Sakellari, D., Prevalence of β-lactam (bla TEM) and metronidazole (nim) resistance genes in the oral cavity of Greek subjects. Open Dent. J. 10 (2016), 89–98.
    • (2016) Open Dent. J. , vol.10 , pp. 89-98
    • Koukos, G.1    Konstantinidis, A.2    Tsalikis, L.3    Arsenakis, M.4    Slini, T.5    Sakellari, D.6
  • 61
    • 84983457243 scopus 로고    scopus 로고
    • Voss, Decolonisation of meticillin-resistant Staphylococcus aureus (MRSA) carriage in adopted children with cleft lip and palate
    • [61] Bos, J., Hopman, M.M., Stuiver, A., Voss, Decolonisation of meticillin-resistant Staphylococcus aureus (MRSA) carriage in adopted children with cleft lip and palate. J. Glob. Antimicrob. Resist. 7 (2016), 28–33.
    • (2016) J. Glob. Antimicrob. Resist. , vol.7 , pp. 28-33
    • Bos, J.1    Hopman, M.M.2    Stuiver, A.3
  • 62
    • 80051550004 scopus 로고    scopus 로고
    • Antimicrobial and DNA-binding activities of the peptide fragments of human lactoferrin and histatin 5 against Streptococcus mutans
    • [62] Huo, L., Zhang, K., Ling, J., Peng, Z., Huang, X., Liu, H., Gu, L., Antimicrobial and DNA-binding activities of the peptide fragments of human lactoferrin and histatin 5 against Streptococcus mutans. Arch. Oral Biol. 56 (2011), 869–876.
    • (2011) Arch. Oral Biol. , vol.56 , pp. 869-876
    • Huo, L.1    Zhang, K.2    Ling, J.3    Peng, Z.4    Huang, X.5    Liu, H.6    Gu, L.7
  • 63
    • 84906266656 scopus 로고    scopus 로고
    • Chemical composition of Enterococcus faecalis in biofilm cells initiated from different physiologic states
    • [63] Liu, H., Xu, Q., Huo, L., Wei, X., Ling, J., Chemical composition of Enterococcus faecalis in biofilm cells initiated from different physiologic states. Folia Microbiol (Praha). 59 (2014), 447–453.
    • (2014) Folia Microbiol (Praha). , vol.59 , pp. 447-453
    • Liu, H.1    Xu, Q.2    Huo, L.3    Wei, X.4    Ling, J.5
  • 64
    • 84876720711 scopus 로고    scopus 로고
    • Expression of human beta defensins (HBDs) 1, 2 and 3 in gingival crevicular fluid of patients affected by localized aggressive periodontitis
    • [64] Ebrahem, M.A., Expression of human beta defensins (HBDs) 1, 2 and 3 in gingival crevicular fluid of patients affected by localized aggressive periodontitis. Saudi Dent. J. 25 (2013), 75–82.
    • (2013) Saudi Dent. J. , vol.25 , pp. 75-82
    • Ebrahem, M.A.1
  • 66
    • 78049442515 scopus 로고    scopus 로고
    • Activity of antimicrobial peptide mimetics in the oral cavity: I. Activity against biofilms of Candida albicans
    • [66] Hua, J., Yamarthy, R., Felsenstein, S., Scott, R.W., Markowitz, K., Diamond, G., Activity of antimicrobial peptide mimetics in the oral cavity: I. Activity against biofilms of Candida albicans. Mol. Oral Microbiol. 25 (2010), 418–425.
    • (2010) Mol. Oral Microbiol. , vol.25 , pp. 418-425
    • Hua, J.1    Yamarthy, R.2    Felsenstein, S.3    Scott, R.W.4    Markowitz, K.5    Diamond, G.6
  • 67
    • 84962120849 scopus 로고
    • Antimicrobial peptides and their interaction with biofilms of medically relevant bacteria
    • [67] Batoni, G., Maisetta, G., Esin, S., Antimicrobial peptides and their interaction with biofilms of medically relevant bacteria. Biochim. Biophys. Acta. 2016 (1858), 1044–1060.
    • (1858) Biochim. Biophys. Acta. , vol.2016 , pp. 1044-1060
    • Batoni, G.1    Maisetta, G.2    Esin, S.3
  • 68
    • 0031975655 scopus 로고    scopus 로고
    • The therapeutic potential of cationic peptides
    • [68] Hancock, R.E., The therapeutic potential of cationic peptides. Expert Opin. Investig. Drugs 7 (1998), 167–174.
    • (1998) Expert Opin. Investig. Drugs , vol.7 , pp. 167-174
    • Hancock, R.E.1
  • 69
    • 3142770748 scopus 로고    scopus 로고
    • Endotoxin neutralizing peptides
    • [69] Jerala, R., Porro, M., Endotoxin neutralizing peptides. Curr. Top. Med. Chem. 4 (2004), 1173–1184.
    • (2004) Curr. Top. Med. Chem. , vol.4 , pp. 1173-1184
    • Jerala, R.1    Porro, M.2
  • 70
    • 34548690015 scopus 로고    scopus 로고
    • Salivary defensins and their importance in oral health and disease
    • [70] Abiko, Y., Saitoh, M., Salivary defensins and their importance in oral health and disease. Curr. Pharm. Des. 13 (2007), 3065–3072.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 3065-3072
    • Abiko, Y.1    Saitoh, M.2
  • 71
    • 79958773596 scopus 로고    scopus 로고
    • Antibacterial peptides: Opportunities for the prevention and treatment of dental caries
    • [71] Pepperney, A., Chikindas, M.L., Antibacterial peptides: Opportunities for the prevention and treatment of dental caries. Probiotics Antimicrob. Proteins, 3, 2011, 68.
    • (2011) Probiotics Antimicrob. Proteins , vol.3 , pp. 68
    • Pepperney, A.1    Chikindas, M.L.2
  • 72
    • 0030949875 scopus 로고    scopus 로고
    • Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • [72] Goldman, M.J., Anderson, G.M., Stolzenberg, E.D., Kari, U.P., Zasloff, M., Wilson, J.M., Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88 (1997), 553–560.
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 73
    • 0033995146 scopus 로고    scopus 로고
    • Synergistic actions of antibacterial neutrophil defensins and cathelicidins
    • [73] Nagaoka, I., Hirota, S., Yomogida, S., Ohwada, A., Hirata, M., Synergistic actions of antibacterial neutrophil defensins and cathelicidins. Inflamm. Res. 49 (2000), 73–79.
    • (2000) Inflamm. Res. , vol.49 , pp. 73-79
    • Nagaoka, I.1    Hirota, S.2    Yomogida, S.3    Ohwada, A.4    Hirata, M.5
  • 74
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • [74] Turner, J., Cho, Y., Dinh, N.N., Waring, A.J., Lehrer, R.I., Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob. Agents Chemother. 42 (1998), 2206–2214.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 75
    • 22944435825 scopus 로고    scopus 로고
    • Antimicrobial peptides in the oral environment: expression and function in health and disease
    • [75] Dale, B.A., Fredericks, L.P., Antimicrobial peptides in the oral environment: expression and function in health and disease. Curr. Issues Mol. Biol. 7 (2005), 119–133.
    • (2005) Curr. Issues Mol. Biol. , vol.7 , pp. 119-133
    • Dale, B.A.1    Fredericks, L.P.2
  • 76
    • 1542513868 scopus 로고    scopus 로고
    • Human-defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms
    • [76] Joly, S., Maze, C., Jr McCray, P.B., Guthmiller, J.M., Human-defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms. J. Clin. Microbiol. 42 (2004), 1024–1029.
    • (2004) J. Clin. Microbiol. , vol.42 , pp. 1024-1029
    • Joly, S.1    Maze, C.2    Jr McCray, P.B.3    Guthmiller, J.M.4
  • 77
    • 60249087859 scopus 로고    scopus 로고
    • In vitro bactericidal activity of recombinant human beta-defensin-3 against pathogenic bacterial strains in human tooth root canal
    • [77] Song, W., Shi, Y., Xiao, M., Lu, H., Qu, T., Li, P., Wu, G., Tian, Y., In vitro bactericidal activity of recombinant human beta-defensin-3 against pathogenic bacterial strains in human tooth root canal. Int. J. Antimicrob. Agents 33 (2009), 237–243.
    • (2009) Int. J. Antimicrob. Agents , vol.33 , pp. 237-243
    • Song, W.1    Shi, Y.2    Xiao, M.3    Lu, H.4    Qu, T.5    Li, P.6    Wu, G.7    Tian, Y.8
  • 78
    • 34548222649 scopus 로고    scopus 로고
    • Antimicrobial activity of truncated alpha-defensin (human neutrophil peptide (HNP)-1) analogues without disulphide bridges
    • [78] Lundy, F.T., Nelson, J., Lockhart, D., Greer, B., Harriott, P., Marley, J.J., Antimicrobial activity of truncated alpha-defensin (human neutrophil peptide (HNP)-1) analogues without disulphide bridges. Mol. Immunol. 45 (2008), 190–193.
    • (2008) Mol. Immunol. , vol.45 , pp. 190-193
    • Lundy, F.T.1    Nelson, J.2    Lockhart, D.3    Greer, B.4    Harriott, P.5    Marley, J.J.6
  • 79
    • 34548230420 scopus 로고    scopus 로고
    • Susceptibility of various oral bacteria to antimicrobial peptides and to phagocytosis by neutrophils
    • [79] Ji, S., Hyun, J., Park, E., Lee, B.L., Kim, K.K., Choi, Y., Susceptibility of various oral bacteria to antimicrobial peptides and to phagocytosis by neutrophils. J. Periodontal Res. 42 (2007), 410–419.
    • (2007) J. Periodontal Res. , vol.42 , pp. 410-419
    • Ji, S.1    Hyun, J.2    Park, E.3    Lee, B.L.4    Kim, K.K.5    Choi, Y.6
  • 80
    • 84862796451 scopus 로고    scopus 로고
    • Antibacterial and neutralizing effect of human beta-defensins on Enterococcus faecalis and Enterococcus faecalis lipoteichoic acid
    • [80] Lee, S.H., Baek, D.H., Antibacterial and neutralizing effect of human beta-defensins on Enterococcus faecalis and Enterococcus faecalis lipoteichoic acid. J. Endod. 38 (2012), 351–356.
    • (2012) J. Endod. , vol.38 , pp. 351-356
    • Lee, S.H.1    Baek, D.H.2
  • 82
    • 33748298908 scopus 로고    scopus 로고
    • Statherin and histatin 1 reduce parotid saliva-promoted Streptococcus mutans strain MT8148 adhesion to hydroxyapatite surfaces
    • [82] Shimotoyodome, A., Kobayashi, H., Tokimitsu, I., Matsukubo, T., Takaesu, Y., Statherin and histatin 1 reduce parotid saliva-promoted Streptococcus mutans strain MT8148 adhesion to hydroxyapatite surfaces. Caries Res. 40 (2006), 403–411.
    • (2006) Caries Res. , vol.40 , pp. 403-411
    • Shimotoyodome, A.1    Kobayashi, H.2    Tokimitsu, I.3    Matsukubo, T.4    Takaesu, Y.5
  • 83
    • 84869096571 scopus 로고    scopus 로고
    • The effect of histatin 5, adsorbed on PMMA and hydroxyapatite, on Candida albicans colonization
    • [83] Vukosavljevic, D., Custodio, W., Del Bel Cury, A.A., Siqueira, W.L., The effect of histatin 5, adsorbed on PMMA and hydroxyapatite, on Candida albicans colonization. Yeast 29 (2012), 459–466.
    • (2012) Yeast , vol.29 , pp. 459-466
    • Vukosavljevic, D.1    Custodio, W.2    Del Bel Cury, A.A.3    Siqueira, W.L.4
  • 85
    • 0035185146 scopus 로고    scopus 로고
    • P-113D, an antimicrobial peptide active against Pseudomonas aeruginosa, retains activity in the presence of sputum from cystic fibrosis patients
    • [85] Sajjan, U.S., Tran, L.T., Sole, N., Rovaldi, C., Akiyama, A., Friden, P.M., Forstner, J.F., Rothstein, D.M., P-113D, an antimicrobial peptide active against Pseudomonas aeruginosa, retains activity in the presence of sputum from cystic fibrosis patients. Antimicrob. Agents Chemother. 45 (2001), 3437–3444.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 3437-3444
    • Sajjan, U.S.1    Tran, L.T.2    Sole, N.3    Rovaldi, C.4    Akiyama, A.5    Friden, P.M.6    Forstner, J.F.7    Rothstein, D.M.8
  • 86
    • 84857677420 scopus 로고    scopus 로고
    • The antibacterial activity of LL-37 against Treponema denticola is dentilisin protease independent and facilitated by the major outer sheath protein virulence factor
    • [86] Rosen, G., Sela, M.N., Bachrach, G., The antibacterial activity of LL-37 against Treponema denticola is dentilisin protease independent and facilitated by the major outer sheath protein virulence factor. Infect. Immun. 80 (2012), 1107–1114.
    • (2012) Infect. Immun. , vol.80 , pp. 1107-1114
    • Rosen, G.1    Sela, M.N.2    Bachrach, G.3
  • 87
    • 77049098530 scopus 로고    scopus 로고
    • Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37
    • [87] Thennarasu, S., Tan, A., Penumatchu, R., Shelburne, C.E., Heyl, D.L., Ramamoorthy, A., Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37. Biophys. J. 98 (2010), 248–257.
    • (2010) Biophys. J. , vol.98 , pp. 248-257
    • Thennarasu, S.1    Tan, A.2    Penumatchu, R.3    Shelburne, C.E.4    Heyl, D.L.5    Ramamoorthy, A.6
  • 89
    • 84874857156 scopus 로고    scopus 로고
    • Direct and indirect antimicrobial activities of neuropeptides and their therapeutic potential
    • [89] Augustyniak, D., Nowak, J., Lundy, F.T., Direct and indirect antimicrobial activities of neuropeptides and their therapeutic potential. Curr. Protein Pept. Sci. 13 (2012), 723–738.
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 723-738
    • Augustyniak, D.1    Nowak, J.2    Lundy, F.T.3
  • 90
    • 49849100430 scopus 로고    scopus 로고
    • Antimicrobial activity of neuropeptides against a range of micro-organisms from skin, oral, respiratory and gastrointestinal tract sites
    • [90] El Karim, I.A., Linden, G.J., Orr, D.F., Lundy, F.T., Antimicrobial activity of neuropeptides against a range of micro-organisms from skin, oral, respiratory and gastrointestinal tract sites. J. Neuroimmunol. 200 (2008), 11–16.
    • (2008) J. Neuroimmunol. , vol.200 , pp. 11-16
    • El Karim, I.A.1    Linden, G.J.2    Orr, D.F.3    Lundy, F.T.4
  • 91
    • 0036372264 scopus 로고    scopus 로고
    • Quantitative analysis of substance P, neurokinin A and calcitonin gene-related peptide in pulp tissue from painful and healthy human teeth
    • [91] Awawdeh, L., Lundy, F.T., Shaw, C., Lamey, P.J., Linden, G.J., Kennedy, J.G., Quantitative analysis of substance P, neurokinin A and calcitonin gene-related peptide in pulp tissue from painful and healthy human teeth. Int. Endod. J. 35 (2002), 30–36.
    • (2002) Int. Endod. J. , vol.35 , pp. 30-36
    • Awawdeh, L.1    Lundy, F.T.2    Shaw, C.3    Lamey, P.J.4    Linden, G.J.5    Kennedy, J.G.6
  • 92
    • 33748546934 scopus 로고    scopus 로고
    • Vasoactive intestinal polypeptide (VIP) and VPAC1 receptor in adult human dental pulp in relation to caries
    • [92] El Karim, I.A., Lamey, P.J., Ardill, J., Linden, G.J., Lundy, F.T., Vasoactive intestinal polypeptide (VIP) and VPAC1 receptor in adult human dental pulp in relation to caries. Arch. Oral Biol. 51 (2006), 849–855.
    • (2006) Arch. Oral Biol. , vol.51 , pp. 849-855
    • El Karim, I.A.1    Lamey, P.J.2    Ardill, J.3    Linden, G.J.4    Lundy, F.T.5
  • 94
    • 68949202993 scopus 로고    scopus 로고
    • The effect of lactoferrin on oral bacterial attachment
    • [94] Arslan, S.Y., Leung, K.P., Wu, C.D., The effect of lactoferrin on oral bacterial attachment. Oral Microbiol. Immunol. 24 (2009), 411–416.
    • (2009) Oral Microbiol. Immunol. , vol.24 , pp. 411-416
    • Arslan, S.Y.1    Leung, K.P.2    Wu, C.D.3
  • 95
    • 23444437935 scopus 로고    scopus 로고
    • A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs
    • [95] Batoni, Y.J., Romanowski, E.G., McDermott, A.M., A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs. Curr. Eye Res. 30 (2005), 505–515.
    • (2005) Curr. Eye Res. , vol.30 , pp. 505-515
    • Batoni, Y.J.1    Romanowski, E.G.2    McDermott, A.M.3
  • 96
    • 84988603422 scopus 로고    scopus 로고
    • Molecular design and genetic optimization of antimicrobial peptides containing unnatural amino acids against antibiotic-resistant bacterial infections
    • Epub ahead of print
    • [96] He, Y., He, X., Molecular design and genetic optimization of antimicrobial peptides containing unnatural amino acids against antibiotic-resistant bacterial infections. Biopolymers, 2016, 10.1002/bip.22885 Epub ahead of print.
    • (2016) Biopolymers
    • He, Y.1    He, X.2
  • 97
    • 78649922290 scopus 로고    scopus 로고
    • Strategies for the discovery and advancement of novel cationic antimicrobial peptides
    • [97] Hadley, E.B., Hancock, R.E., Strategies for the discovery and advancement of novel cationic antimicrobial peptides. Curr. Top Med. Chem. 10 (2010), 1872–1881.
    • (2010) Curr. Top Med. Chem. , vol.10 , pp. 1872-1881
    • Hadley, E.B.1    Hancock, R.E.2
  • 98
    • 80051546187 scopus 로고    scopus 로고
    • Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?
    • [98] Brogden, N.K., Brogden, K.A., Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?. Int. J. Antimicrob. Agents. 38 (2011), 217–225.
    • (2011) Int. J. Antimicrob. Agents. , vol.38 , pp. 217-225
    • Brogden, N.K.1    Brogden, K.A.2
  • 99
    • 84868120048 scopus 로고    scopus 로고
    • Antimicrobial peptides for therapeutic applications: a review
    • [99] Seo, M.D., Won, H.S., Kim, J.H., Mishig-Ochir, T., Lee, B.J., Antimicrobial peptides for therapeutic applications: a review. Molecules 17 (2012), 12276–12286.
    • (2012) Molecules , vol.17 , pp. 12276-12286
    • Seo, M.D.1    Won, H.S.2    Kim, J.H.3    Mishig-Ochir, T.4    Lee, B.J.5
  • 103
    • 84955057534 scopus 로고    scopus 로고
    • In silico design of antimicrobial peptides
    • [103] Maccari, G., Di Luca, M., Nifosì, R., In silico design of antimicrobial peptides. Methods Mol. Biol. 1268 (2015), 195–219.
    • (2015) Methods Mol. Biol. , vol.1268 , pp. 195-219
    • Maccari, G.1    Di Luca, M.2    Nifosì, R.3
  • 104
    • 85011843832 scopus 로고    scopus 로고
    • Design and application of antimicrobial peptide conjugates
    • [104] Reinhardt, A., Neundorf, I., Design and application of antimicrobial peptide conjugates. Int. J. Mol. Sci., 17, 2016, 701.
    • (2016) Int. J. Mol. Sci. , vol.17 , pp. 701
    • Reinhardt, A.1    Neundorf, I.2
  • 105
    • 47749116861 scopus 로고    scopus 로고
    • Synthetic antimicrobial peptidomimetics with therapeutic potential
    • [105] Haug, B.E., Stensen, W., Kalaaji, M., Rekdal, Ø., Svendsen, J.S., Synthetic antimicrobial peptidomimetics with therapeutic potential. J. Med. Chem. 51 (2008), 4306–4314.
    • (2008) J. Med. Chem. , vol.51 , pp. 4306-4314
    • Haug, B.E.1    Stensen, W.2    Kalaaji, M.3    Rekdal, Ø.4    Svendsen, J.S.5
  • 106
    • 84867383554 scopus 로고    scopus 로고
    • Recent development of small antimicrobial peptidomimetics
    • [106] Niu, Y., Wang, R.E., Wu, H., Cai, J., Recent development of small antimicrobial peptidomimetics. Future Med. Chem. 4 (2012), 1853–1862.
    • (2012) Future Med. Chem. , vol.4 , pp. 1853-1862
    • Niu, Y.1    Wang, R.E.2    Wu, H.3    Cai, J.4
  • 107
    • 84907879304 scopus 로고    scopus 로고
    • Peptidomimetics as a new generation of antimicrobial agents: current progress
    • [107] Méndez-Samperio, P., Peptidomimetics as a new generation of antimicrobial agents: current progress. Infect. Drug Resist. 7 (2014), 229–237.
    • (2014) Infect. Drug Resist. , vol.7 , pp. 229-237
    • Méndez-Samperio, P.1
  • 109
    • 78650294475 scopus 로고    scopus 로고
    • Effect of the antimicrobial decapeptide KSL on the growth of oral pathogens and Streptococcus mutans biofilm
    • [109] Liu, Y., Wang, L., Zhou, X., Hu, S., Zhang, S., Wu, H., Effect of the antimicrobial decapeptide KSL on the growth of oral pathogens and Streptococcus mutans biofilm. Int. J. Antimicrob. Agents. 37 (2011), 33–38.
    • (2011) Int. J. Antimicrob. Agents. , vol.37 , pp. 33-38
    • Liu, Y.1    Wang, L.2    Zhou, X.3    Hu, S.4    Zhang, S.5    Wu, H.6
  • 112
    • 84954096190 scopus 로고    scopus 로고
    • Biohybrid polymer-antimicrobial peptide medium against Enterococcus faecalis
    • [112] Eckhard, L.H., Sol, A., Abtew, E., Shai, Y., Domb, A.J., Bachrach, G., Beyth, N., Biohybrid polymer-antimicrobial peptide medium against Enterococcus faecalis. PLoS ONE, 9, 2014, e109413.
    • (2014) PLoS ONE , vol.9 , pp. e109413
    • Eckhard, L.H.1    Sol, A.2    Abtew, E.3    Shai, Y.4    Domb, A.J.5    Bachrach, G.6    Beyth, N.7
  • 114
    • 0032957681 scopus 로고    scopus 로고
    • Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane
    • [114] Wu, M., Hancock, R.E., Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. J. Biol. Chem. 274 (1999), 29–35.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29-35
    • Wu, M.1    Hancock, R.E.2
  • 115
    • 67649277613 scopus 로고    scopus 로고
    • Solution NMR studies of amphibian antimicrobial peptides: linking structure to function?
    • [115] Haney, E.F., Hunter, H.N., Matsuzaki, K., Vogel, H.J., Solution NMR studies of amphibian antimicrobial peptides: linking structure to function?. Biochim. Biophys. Acta. 1788 (2009), 1639–1655.
    • (2009) Biochim. Biophys. Acta. , vol.1788 , pp. 1639-1655
    • Haney, E.F.1    Hunter, H.N.2    Matsuzaki, K.3    Vogel, H.J.4
  • 119
    • 1842478127 scopus 로고    scopus 로고
    • A new group of antifungal and antibacterial lipopeptides derived from non-membrane active peptides conjugated to palmitic acid
    • [119] Avrahami, D., Shai, Y., A new group of antifungal and antibacterial lipopeptides derived from non-membrane active peptides conjugated to palmitic acid. J. Biol. Chem. 279 (2004), 12277–12285.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12277-12285
    • Avrahami, D.1    Shai, Y.2
  • 120
    • 59749089160 scopus 로고    scopus 로고
    • Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37
    • [120] Stromstedt, A.A., Pasupuleti, M., Schmidtchen, A., Malmsten, M., Evaluation of strategies for improving proteolytic resistance of antimicrobial peptides by using variants of EFK17, an internal segment of LL-37. Antimicrob. Agents Chemother. 53 (2009), 593–602.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 593-602
    • Stromstedt, A.A.1    Pasupuleti, M.2    Schmidtchen, A.3    Malmsten, M.4
  • 121
    • 23444451770 scopus 로고    scopus 로고
    • High-throughput generation of small antibacterial peptides with improved activity
    • [121] Hilpert, K., Volkmer-Engert, R., Walter, T., Hancock, R.E., High-throughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 23 (2005), 1008–1012.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1008-1012
    • Hilpert, K.1    Volkmer-Engert, R.2    Walter, T.3    Hancock, R.E.4
  • 122
    • 84891605011 scopus 로고    scopus 로고
    • Antimicrobial and anti-biofilm effect of Bac8c on major bacteria associated with dental caries and Streptococcus mutans biofilms
    • [122] Ding, Y., Wang, W., Fan, M., Tong, Z., Kuang, R., Jiang, W., Ni, L., Antimicrobial and anti-biofilm effect of Bac8c on major bacteria associated with dental caries and Streptococcus mutans biofilms. Peptides 52 (2014), 61–67.
    • (2014) Peptides , vol.52 , pp. 61-67
    • Ding, Y.1    Wang, W.2    Fan, M.3    Tong, Z.4    Kuang, R.5    Jiang, W.6    Ni, L.7
  • 123
    • 84928802858 scopus 로고    scopus 로고
    • Peptide IDR-1018: modulating the immune system and targeting bacterial biofilms to treat antibiotic-resistant bacterial infections
    • [123] Mansour, S.C., de la Fuente-Núñez, C., Hancock, R.E., Peptide IDR-1018: modulating the immune system and targeting bacterial biofilms to treat antibiotic-resistant bacterial infections. J. Pept. Sci. 21 (2015), 323–329.
    • (2015) J. Pept. Sci. , vol.21 , pp. 323-329
    • Mansour, S.C.1    de la Fuente-Núñez, C.2    Hancock, R.E.3
  • 125
    • 84879570321 scopus 로고    scopus 로고
    • The innate defense regulator peptides IDR-HH2, IDR-1002, and IDR-1018 modulate human neutrophil functions
    • [125] Niyonsaba, F., Madera, L., Afacan, N., Okumura, K., Ogawa, H., Hancock, R.E., The innate defense regulator peptides IDR-HH2, IDR-1002, and IDR-1018 modulate human neutrophil functions. J. Leukoc. Biol. 94 (2013), 159–170.
    • (2013) J. Leukoc. Biol. , vol.94 , pp. 159-170
    • Niyonsaba, F.1    Madera, L.2    Afacan, N.3    Okumura, K.4    Ogawa, H.5    Hancock, R.E.6
  • 126
    • 84940512885 scopus 로고    scopus 로고
    • Treatment of oral multispecies biofilms by an anti-biofilm peptide
    • [126] Wang, Z., de la Fuente-Nunez, C., Shen, Y., Haapasalo, M., Hancock, R.E., Treatment of oral multispecies biofilms by an anti-biofilm peptide. PLoS ONE, 10, 2015, e0132512.
    • (2015) PLoS ONE , vol.10 , pp. e0132512
    • Wang, Z.1    de la Fuente-Nunez, C.2    Shen, Y.3    Haapasalo, M.4    Hancock, R.E.5
  • 127
    • 0028475512 scopus 로고
    • Microbial ecology of dental plaque and its significance in health and disease
    • [127] Marsh, P.D., Microbial ecology of dental plaque and its significance in health and disease. Adv. Dent. Res. 8 (1994), 263–271.
    • (1994) Adv. Dent. Res. , vol.8 , pp. 263-271
    • Marsh, P.D.1
  • 128
    • 2642547950 scopus 로고    scopus 로고
    • Dental plaque as a microbial biofilm
    • [128] Marsh, P.D., Dental plaque as a microbial biofilm. Caries Res. 38 (2004), 204–211.
    • (2004) Caries Res. , vol.38 , pp. 204-211
    • Marsh, P.D.1
  • 129
    • 33750584025 scopus 로고    scopus 로고
    • Targeted killing of Streptococcus mutans by a pheromone-guided “smart” antimicrobial peptide
    • [129] Eckert, R., He, J., Yarbrough, D.K., Qi, F., Anderson, M.H., Shi, W., Targeted killing of Streptococcus mutans by a pheromone-guided “smart” antimicrobial peptide. Antimicrob. Agents Chemother. 50 (2006), 3651–3657.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 3651-3657
    • Eckert, R.1    He, J.2    Yarbrough, D.K.3    Qi, F.4    Anderson, M.H.5    Shi, W.6
  • 130
    • 77951236068 scopus 로고    scopus 로고
    • Systematic approach to optimizing specifically Targeted Antimicrobial Peptides against Streptococcus mutans
    • [130] He, J., Yarbrough, D.K., Kreth, J., Anderson, M.H., Shi, W., Eckert, R., Systematic approach to optimizing specifically Targeted Antimicrobial Peptides against Streptococcus mutans. Antimicrob. Agents Chemother. 54 (2010), 2143–2151.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 2143-2151
    • He, J.1    Yarbrough, D.K.2    Kreth, J.3    Anderson, M.H.4    Shi, W.5    Eckert, R.6
  • 131
    • 79959213007 scopus 로고    scopus 로고
    • Selective membrane disruption: mode of action of C16G2, a specifically targeted antimicrobial peptide
    • [131] Kaplan, C.W., Sim, J.H., Shah, K.R., Kolesnikova-Kaplan, A., Shi, W., Eckert, R., Selective membrane disruption: mode of action of C16G2, a specifically targeted antimicrobial peptide. Antimicrob. Agents Chemother. 55 (2011), 3446–3452.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 3446-3452
    • Kaplan, C.W.1    Sim, J.H.2    Shah, K.R.3    Kolesnikova-Kaplan, A.4    Shi, W.5    Eckert, R.6
  • 132
    • 84865273333 scopus 로고    scopus 로고
    • Targeted antimicrobial treatment to re-establish a healthy microbial flora for long-term protection
    • [132] Eckert, R., Sullivan, R., Shi, W., Targeted antimicrobial treatment to re-establish a healthy microbial flora for long-term protection. Adv. Dent. Res. 24 (2012), 94–97.
    • (2012) Adv. Dent. Res. , vol.24 , pp. 94-97
    • Eckert, R.1    Sullivan, R.2    Shi, W.3
  • 134
    • 80051798579 scopus 로고    scopus 로고
    • Clinical efficacy of a specifically targeted antimicrobial peptide mouth rinse: targeted elimination of Streptococcus mutans and prevention of demineralization
    • [134] Sullivan, R., Santarpia, P., Lavender, S., Gittins, E., Liu, Z., Anderson, M.H., He, J., Shi, W., Eckert, R., Clinical efficacy of a specifically targeted antimicrobial peptide mouth rinse: targeted elimination of Streptococcus mutans and prevention of demineralization. Caries Res. 45 (2011), 415–428.
    • (2011) Caries Res. , vol.45 , pp. 415-428
    • Sullivan, R.1    Santarpia, P.2    Lavender, S.3    Gittins, E.4    Liu, Z.5    Anderson, M.H.6    He, J.7    Shi, W.8    Eckert, R.9
  • 135
    • 12344327691 scopus 로고    scopus 로고
    • Life as an endodontic pathogen. Etiological differences between untreated and root-filled root canals
    • [135] Sundqvist, G., Figdor, D., Life as an endodontic pathogen. Etiological differences between untreated and root-filled root canals. Endod. Topics 6 (2003), 3–28.
    • (2003) Endod. Topics , vol.6 , pp. 3-28
    • Sundqvist, G.1    Figdor, D.2
  • 136
    • 70350381756 scopus 로고    scopus 로고
    • Diversity of endodontic microbiota revisited
    • [136] Jr Siqueira, J.F., Rôças, I.N., Diversity of endodontic microbiota revisited. J. Dent. Res. 88 (2009), 969–981.
    • (2009) J. Dent. Res. , vol.88 , pp. 969-981
    • Jr Siqueira, J.F.1    Rôças, I.N.2
  • 138
    • 0031986907 scopus 로고    scopus 로고
    • Microbiological status of root-filled teeth with apical periodontitis
    • [138] Molander, A., Reit, C., Dahlén, G., Kvist, T., Microbiological status of root-filled teeth with apical periodontitis. Int. Endod. J. 31 (1998), 1–7.
    • (1998) Int. Endod. J. , vol.31 , pp. 1-7
    • Molander, A.1    Reit, C.2    Dahlén, G.3    Kvist, T.4
  • 139
  • 140
    • 84902553178 scopus 로고    scopus 로고
    • Microbial diversity in persistent root canal infections investigated by checkerboard DNA-DNA hybridization
    • [140] Murad, C.F., Sassone, L.M., Faveri, M., Jr Hirata, R., Figueiredo, L., Feres, M., Microbial diversity in persistent root canal infections investigated by checkerboard DNA-DNA hybridization. J. Endod. 40 (2014), 899–906.
    • (2014) J. Endod. , vol.40 , pp. 899-906
    • Murad, C.F.1    Sassone, L.M.2    Faveri, M.3    Jr Hirata, R.4    Figueiredo, L.5    Feres, M.6
  • 141
    • 84975166995 scopus 로고    scopus 로고
    • Nisin as a food preservative: Part 1: Physicochemical properties, antimicrobial activity, and main uses
    • [141] Gharsallaoui, A., Oulahal, N., Joly, C., Degraeve, P., Nisin as a food preservative: Part 1: Physicochemical properties, antimicrobial activity, and main uses. Crit. Rev. Food Sci. Nutr. 56 (2016), 1262–1274.
    • (2016) Crit. Rev. Food Sci. Nutr. , vol.56 , pp. 1262-1274
    • Gharsallaoui, A.1    Oulahal, N.2    Joly, C.3    Degraeve, P.4
  • 142
    • 84974529002 scopus 로고    scopus 로고
    • Nisin as a food preservative: Part 2: Antimicrobial polymer materials containing nisin
    • [142] Gharsallaoui, A., Joly, C., Oulahal, N., Degraeve, P., Nisin as a food preservative: Part 2: Antimicrobial polymer materials containing nisin. Crit. Rev. Food Sci. Nutr. 56 (2016), 1275–1289.
    • (2016) Crit. Rev. Food Sci. Nutr. , vol.56 , pp. 1275-1289
    • Gharsallaoui, A.1    Joly, C.2    Oulahal, N.3    Degraeve, P.4
  • 143
    • 48449097450 scopus 로고    scopus 로고
    • The bacteriocin nisin, an effective agent for the treatment of staphylococcal mastitis during lactation
    • [143] Fernandez, L., Delgado, S., Herrero, H., Maldonado, A., Rodríguez, J.M., The bacteriocin nisin, an effective agent for the treatment of staphylococcal mastitis during lactation. J. Hum. Lact. 24 (2008), 311–316.
    • (2008) J. Hum. Lact. , vol.24 , pp. 311-316
    • Fernandez, L.1    Delgado, S.2    Herrero, H.3    Maldonado, A.4    Rodríguez, J.M.5
  • 144
    • 0029963747 scopus 로고    scopus 로고
    • The antistaphylococcal effect of nisin in a suitable vehicle: a potential therapy for atopic dermatitis in man
    • [144] Valenta, C., Bernkop-Schnurch, A., Rigler, H.P., The antistaphylococcal effect of nisin in a suitable vehicle: a potential therapy for atopic dermatitis in man. J. Pharm. Pharmacol. 48 (1996), 988–991.
    • (1996) J. Pharm. Pharmacol. , vol.48 , pp. 988-991
    • Valenta, C.1    Bernkop-Schnurch, A.2    Rigler, H.P.3
  • 145
    • 58149295989 scopus 로고    scopus 로고
    • Nisin F in the treatment of respiratory tract infections caused by Staphylococcus aureus
    • [145] De Kwaadsteniet, M., Doeschate, K.T., Dicks, L.M., Nisin F in the treatment of respiratory tract infections caused by Staphylococcus aureus. Lett. Appl. Microbiol. 48 (2009), 65–70.
    • (2009) Lett. Appl. Microbiol. , vol.48 , pp. 65-70
    • De Kwaadsteniet, M.1    Doeschate, K.T.2    Dicks, L.M.3
  • 146
    • 77957840141 scopus 로고    scopus 로고
    • Nisin inhibits dental caries-associated microorganism in vitro
    • [146] Tong, Z., Dong, L., Zhou, L., Tao, R., Ni, L., Nisin inhibits dental caries-associated microorganism in vitro. Peptides 31 (2010), 2003–2008.
    • (2010) Peptides , vol.31 , pp. 2003-2008
    • Tong, Z.1    Dong, L.2    Zhou, L.3    Tao, R.4    Ni, L.5
  • 147
    • 84936994910 scopus 로고    scopus 로고
    • Antimicrobial nisin acts against saliva derived multi-species biofilms without cytotoxicity to human oral cells
    • [147] Shin, J.M., Ateia, I., Paulus, J.R., Liu, H., Fenno, J.C., Rickard, A.H., Kapila, Y.L., Antimicrobial nisin acts against saliva derived multi-species biofilms without cytotoxicity to human oral cells. Front. Microbiol., 6, 2015, 617.
    • (2015) Front. Microbiol. , vol.6 , pp. 617
    • Shin, J.M.1    Ateia, I.2    Paulus, J.R.3    Liu, H.4    Fenno, J.C.5    Rickard, A.H.6    Kapila, Y.L.7
  • 148
    • 80054078454 scopus 로고    scopus 로고
    • An in vitro synergetic evaluation of the use of nisin and sodium fluoride or chlorhexidine against Streptococcus mutans
    • [148] Tong, Z., Zhou, L., Jiang, W., Kuang, R., Li, J., Tao, R., Ni, L., An in vitro synergetic evaluation of the use of nisin and sodium fluoride or chlorhexidine against Streptococcus mutans. Peptides 32 (2011), 2021–2026.
    • (2011) Peptides , vol.32 , pp. 2021-2026
    • Tong, Z.1    Zhou, L.2    Jiang, W.3    Kuang, R.4    Li, J.5    Tao, R.6    Ni, L.7
  • 149
    • 84903318216 scopus 로고    scopus 로고
    • An in vitro study on the effect of free amino acids alone or in combination with nisin on biofilms as well as on planktonic bacteria of Streptococcus mutans
    • [149] Tong, Z., Zhang, L., Ling, J., Jian, Y., Huang, L., Deng, D., An in vitro study on the effect of free amino acids alone or in combination with nisin on biofilms as well as on planktonic bacteria of Streptococcus mutans. PLoS ONE, 9, 2014, e99513.
    • (2014) PLoS ONE , vol.9 , pp. e99513
    • Tong, Z.1    Zhang, L.2    Ling, J.3    Jian, Y.4    Huang, L.5    Deng, D.6
  • 150
    • 4644228442 scopus 로고    scopus 로고
    • An in-vitro investigation of the antibacterial effect of nisin in root canals and canal wall radicular dentine
    • [150] Turner, S.R., Love, R.M., Lyons, K.M., An in-vitro investigation of the antibacterial effect of nisin in root canals and canal wall radicular dentine. Int. Endod. J. 37 (2004), 664–671.
    • (2004) Int. Endod. J. , vol.37 , pp. 664-671
    • Turner, S.R.1    Love, R.M.2    Lyons, K.M.3
  • 151
    • 84897400241 scopus 로고    scopus 로고
    • Effects of intracanal irrigant MTAD Combined with nisin at sub-minimum inhibitory concentration levels on Enterococcus faecalis growth and the expression of pathogenic genes
    • [151] Tong, Z., Huang, L., Ling, J., Mao, X., Ning, Y., Deng, D., Effects of intracanal irrigant MTAD Combined with nisin at sub-minimum inhibitory concentration levels on Enterococcus faecalis growth and the expression of pathogenic genes. PLoS ONE, 9, 2014, e90235.
    • (2014) PLoS ONE , vol.9 , pp. e90235
    • Tong, Z.1    Huang, L.2    Ling, J.3    Mao, X.4    Ning, Y.5    Deng, D.6
  • 152
    • 84876668690 scopus 로고    scopus 로고
    • The effect of MTADN on 10 Enterococcus faecalis isolates and biofilm: an in vitro study
    • [152] Tong, Z., Ling, J., Lin, Z., Li, X., Mu, Y., The effect of MTADN on 10 Enterococcus faecalis isolates and biofilm: an in vitro study. J. Endod. 39 (2013), 674–678.
    • (2013) J. Endod. , vol.39 , pp. 674-678
    • Tong, Z.1    Ling, J.2    Lin, Z.3    Li, X.4    Mu, Y.5
  • 153
    • 84858332734 scopus 로고    scopus 로고
    • In vitro evaluation of MTAD and nisin in combination against common pathogens associated with root canal infection
    • [153] Tong, Z., Zhou, L., Kuang, R., Lv, H., Qu, T., Ni, L., In vitro evaluation of MTAD and nisin in combination against common pathogens associated with root canal infection. J. Endod. 38 (2012), 490–494.
    • (2012) J. Endod. , vol.38 , pp. 490-494
    • Tong, Z.1    Zhou, L.2    Kuang, R.3    Lv, H.4    Qu, T.5    Ni, L.6
  • 154
    • 79960456028 scopus 로고    scopus 로고
    • In vitro evaluation of the antibacterial activities of MTAD in combination with nisin against Enterococcus faecalis
    • [154] Tong, Z., Zhou, L., Li, J., Jiang, W., Ma, L., Ni, L., In vitro evaluation of the antibacterial activities of MTAD in combination with nisin against Enterococcus faecalis. J. Endod. 37 (2011), 1116–1120.
    • (2011) J. Endod. , vol.37 , pp. 1116-1120
    • Tong, Z.1    Zhou, L.2    Li, J.3    Jiang, W.4    Ma, L.5    Ni, L.6
  • 155
    • 0025840478 scopus 로고
    • Nisin treatment for inactivation of Salmonella species and other gram-negative bacteria
    • [155] Stevens, K.A., Sheldon, B.W., Klapes, N.A., Klaenhammer, T.R., Nisin treatment for inactivation of Salmonella species and other gram-negative bacteria. Appl. Environ. Microbiol. 57 (1991), 3613–3615.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 3613-3615
    • Stevens, K.A.1    Sheldon, B.W.2    Klapes, N.A.3    Klaenhammer, T.R.4
  • 156
    • 84895895268 scopus 로고    scopus 로고
    • An in vitro study on the effects of nisin on the antibacterial activities of 18 antibiotics against Enterococcus faecalis
    • [156] Tong, Z., Zhang, Y., Ling, J., Ma, J., Huang, L., Zhang, L., An in vitro study on the effects of nisin on the antibacterial activities of 18 antibiotics against Enterococcus faecalis. PLoS ONE, 9, 2014, e89209.
    • (2014) PLoS ONE , vol.9 , pp. e89209
    • Tong, Z.1    Zhang, Y.2    Ling, J.3    Ma, J.4    Huang, L.5    Zhang, L.6
  • 157
    • 80051552897 scopus 로고    scopus 로고
    • Beta-defensins: what are they really doing in the oral cavity?
    • [157] Diamond, G., Ryan, L., Beta-defensins: what are they really doing in the oral cavity?. Oral Dis. 17 (2011), 628–635.
    • (2011) Oral Dis. , vol.17 , pp. 628-635
    • Diamond, G.1    Ryan, L.2
  • 158
    • 0034020351 scopus 로고    scopus 로고
    • Inducible expression of human beta-defensin 2 by Fusobacterium nucleatum in oral epithelial cells: multiple signaling pathways and role of commensal bacteria in innate immunity and the epithelial barrier
    • [158] Krisanaprakornkit, S., Kimball, J.R., Weinberg, A., Darveau, R.P., Bainbridge, B.W., Dale, B.A., Inducible expression of human beta-defensin 2 by Fusobacterium nucleatum in oral epithelial cells: multiple signaling pathways and role of commensal bacteria in innate immunity and the epithelial barrier. Infect. Immun. 68 (2000), 2907–2915.
    • (2000) Infect. Immun. , vol.68 , pp. 2907-2915
    • Krisanaprakornkit, S.1    Kimball, J.R.2    Weinberg, A.3    Darveau, R.P.4    Bainbridge, B.W.5    Dale, B.A.6
  • 159
    • 71049152434 scopus 로고    scopus 로고
    • Effect of proinflammatory cytokines on the expression and regulation of human beta-defensin 2 in human dental pulp cells
    • [159] Kim, Y.S., Min, K.S., Lee, S.I., Shin, S.J., Shin, K.S., Kim, E.C., Effect of proinflammatory cytokines on the expression and regulation of human beta-defensin 2 in human dental pulp cells. J. Endod. 36 (2010), 64–69.
    • (2010) J. Endod. , vol.36 , pp. 64-69
    • Kim, Y.S.1    Min, K.S.2    Lee, S.I.3    Shin, S.J.4    Shin, K.S.5    Kim, E.C.6
  • 160
    • 80054077112 scopus 로고    scopus 로고
    • Role of SIRT1 in heat stress- and lipopolysaccharide-induced immune and defense gene expression in human dental pulp cells
    • [160] Lee, S.I., Min, K.S., Bae, W.J., Lee, Y.M., Lee, S.Y., Lee, E.S., Kim, E.C., Role of SIRT1 in heat stress- and lipopolysaccharide-induced immune and defense gene expression in human dental pulp cells. J. Endod. 37 (2011), 1525–1530.
    • (2011) J. Endod. , vol.37 , pp. 1525-1530
    • Lee, S.I.1    Min, K.S.2    Bae, W.J.3    Lee, Y.M.4    Lee, S.Y.5    Lee, E.S.6    Kim, E.C.7
  • 161
    • 78751641324 scopus 로고    scopus 로고
    • Caries induced cytokine network in the odontoblast layer of human teeth
    • [161] Horst, O.V., Horst, J.A., Samudrala, R., Dale, B.A., Caries induced cytokine network in the odontoblast layer of human teeth. BMC Immunol., 12, 2011, 9.
    • (2011) BMC Immunol. , vol.12 , pp. 9
    • Horst, O.V.1    Horst, J.A.2    Samudrala, R.3    Dale, B.A.4
  • 162
    • 63449139717 scopus 로고    scopus 로고
    • Gene expression of human beta-defensins in healthy and inflamed human dental pulps
    • [162] Paris, S., Wolgin, M., Kielbassa, A.M., Pries, A., Zakrzewicz, A., Gene expression of human beta-defensins in healthy and inflamed human dental pulps. J. Endod. 35 (2009), 520–523.
    • (2009) J. Endod. , vol.35 , pp. 520-523
    • Paris, S.1    Wolgin, M.2    Kielbassa, A.M.3    Pries, A.4    Zakrzewicz, A.5
  • 163
    • 84932197431 scopus 로고    scopus 로고
    • Muramyl dipeptide activates human beta defensin 2 and pro-inflammatory mediators through Toll-like receptors and NLRP3 inflammasomes in human dental pulp cells
    • [163] Lee, S.I., Kang, S.K., Jung, H.J., Chun, Y.H., Kwon, Y.D., Kim, E.C., Muramyl dipeptide activates human beta defensin 2 and pro-inflammatory mediators through Toll-like receptors and NLRP3 inflammasomes in human dental pulp cells. Clin. Oral Investig. 19 (2015), 1419–1428.
    • (2015) Clin. Oral Investig. , vol.19 , pp. 1419-1428
    • Lee, S.I.1    Kang, S.K.2    Jung, H.J.3    Chun, Y.H.4    Kwon, Y.D.5    Kim, E.C.6
  • 170
    • 0034585802 scopus 로고    scopus 로고
    • Salivary histatin 5 and its similarities to the other antimicrobial proteins in human saliva
    • [170] Edgerton, M., Koshlukova, S.E., Salivary histatin 5 and its similarities to the other antimicrobial proteins in human saliva. Adv. Dent. Res. 14 (2000), 16–21.
    • (2000) Adv. Dent. Res. , vol.14 , pp. 16-21
    • Edgerton, M.1    Koshlukova, S.E.2
  • 172
    • 0029450014 scopus 로고
    • Functional comparison of native and recombinant human salivary histatin 1
    • [172] Driscoll, J., Zuo, Y., Xu, T., Choi, J.R., Troxler, R.F., Oppenheim, F.G., Functional comparison of native and recombinant human salivary histatin 1. J. Dent. Res. 74 (1995), 1837–1844.
    • (1995) J. Dent. Res. , vol.74 , pp. 1837-1844
    • Driscoll, J.1    Zuo, Y.2    Xu, T.3    Choi, J.R.4    Troxler, R.F.5    Oppenheim, F.G.6
  • 175
    • 79951597464 scopus 로고    scopus 로고
    • Histatin 1 resists proteolytic degradation when adsorbed to hydroxyapatite
    • [175] McDonald, E.E., Goldberg, H.A., Tabbara, N., Mendes, F.M., Siqueira, W.L., Histatin 1 resists proteolytic degradation when adsorbed to hydroxyapatite. J. Dent. Res. 90 (2011), 268–272.
    • (2011) J. Dent. Res. , vol.90 , pp. 268-272
    • McDonald, E.E.1    Goldberg, H.A.2    Tabbara, N.3    Mendes, F.M.4    Siqueira, W.L.5
  • 176
    • 33745194211 scopus 로고    scopus 로고
    • Molecular mechanisms of bacterial resistance to antimicrobial peptides
    • [176] Kraus, D., Peschel, A., Molecular mechanisms of bacterial resistance to antimicrobial peptides. Curr Top Microbiol Immunol 306 (2006), 231–250.
    • (2006) Curr Top Microbiol Immunol , vol.306 , pp. 231-250
    • Kraus, D.1    Peschel, A.2
  • 177
    • 33745206370 scopus 로고    scopus 로고
    • Bacterial evasion of antimicrobial peptides by biofilm formation
    • [177] Otto, M., Bacterial evasion of antimicrobial peptides by biofilm formation. Curr Top Microbiol Immunol 306 (2006), 251–258.
    • (2006) Curr Top Microbiol Immunol , vol.306 , pp. 251-258
    • Otto, M.1
  • 178
    • 0028114658 scopus 로고
    • How bacteria resist killing by host defense peptides
    • [178] Groisman, E.A., How bacteria resist killing by host defense peptides. Trends Microbiol. Sci. 2 (1994), 444–448.
    • (1994) Trends Microbiol. Sci. , vol.2 , pp. 444-448
    • Groisman, E.A.1
  • 180
    • 25144434489 scopus 로고    scopus 로고
    • Antimicrobial peptide resistance mechanisms of human bacterial pathogens
    • [180] Nizet, V., Antimicrobial peptide resistance mechanisms of human bacterial pathogens. Curr. Issues Mol. Biol. 8 (2006), 11–26.
    • (2006) Curr. Issues Mol. Biol. , vol.8 , pp. 11-26
    • Nizet, V.1
  • 182
    • 84966400415 scopus 로고    scopus 로고
    • Bacterial evasion of host antimicrobial peptide defenses
    • [182] Cole, J.N., Nizet, V., Bacterial evasion of host antimicrobial peptide defenses. Microbiol. Spectr., 4, 2016, 10.1128/microbiolspec.VMBF-0006-2015.
    • (2016) Microbiol. Spectr. , vol.4
    • Cole, J.N.1    Nizet, V.2
  • 183
    • 84943661837 scopus 로고
    • Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogens
    • [183] LaRock, C.N., Nizet, V., Cationic antimicrobial peptide resistance mechanisms of streptococcal pathogens. Biochim. Biophys Acta. 2015 (1848), 3047–3054.
    • (1848) Biochim. Biophys Acta. , vol.2015 , pp. 3047-3054
    • LaRock, C.N.1    Nizet, V.2
  • 184
    • 84943816958 scopus 로고    scopus 로고
    • Defensive remodeling: How bacterial surface properties and biofilm formation promote resistance to antimicrobial peptides
    • [184] Nuri, R., Shprung, T., Shai, Y., Defensive remodeling: How bacterial surface properties and biofilm formation promote resistance to antimicrobial peptides. Biochim. Biophys. Acta. 1848:11 Pt B (2015), 3089–3100.
    • (2015) Biochim. Biophys. Acta. , vol.1848 , Issue.11 , pp. 3089-3100
    • Nuri, R.1    Shprung, T.2    Shai, Y.3
  • 185
    • 84943665377 scopus 로고    scopus 로고
    • On the in vivo significance of bacterial resistance to antimicrobial peptides
    • [185] Bauer, M.E., Shafer, W.M., On the in vivo significance of bacterial resistance to antimicrobial peptides. Biochim. Biophys. Acta. 1848:11 Pt B (2015), 3101–3111.
    • (2015) Biochim. Biophys. Acta. , vol.1848 , Issue.11 , pp. 3101-3111
    • Bauer, M.E.1    Shafer, W.M.2
  • 186
    • 84974604292 scopus 로고    scopus 로고
    • Anti-biofilm peptides as a new weapon in antimicrobial warfare
    • [186] Pletzer, D., Coleman, S.R., Hancock, R.E., Anti-biofilm peptides as a new weapon in antimicrobial warfare. Curr. Opin. Microbiol. 33 (2016), 35–40.
    • (2016) Curr. Opin. Microbiol. , vol.33 , pp. 35-40
    • Pletzer, D.1    Coleman, S.R.2    Hancock, R.E.3
  • 187
    • 0025690257 scopus 로고
    • In vitro sensitivity of oral, gram-negative, facultative bacteria to the bactericidal activity of human neutrophil defensins
    • [187] Miyasaki, K.T., Bodeau, A.L., Ganz, T., Selsted, M.E., Lehrer, R.I., In vitro sensitivity of oral, gram-negative, facultative bacteria to the bactericidal activity of human neutrophil defensins. Infect. Immun. 58 (1990), 3934–3940.
    • (1990) Infect. Immun. , vol.58 , pp. 3934-3940
    • Miyasaki, K.T.1    Bodeau, A.L.2    Ganz, T.3    Selsted, M.E.4    Lehrer, R.I.5
  • 188
    • 21244433198 scopus 로고    scopus 로고
    • Susceptibilities of periodontopathogenic and cariogenic bacteria to antibacterial peptides, beta-defensins and LL37, produced by human epithelial cells
    • [188] Ouhara, K., Komatsuzawa, H., Yamada, S., Shiba, H., Fujiwara, T., Ohara, M., Sayama, K., Hashimoto, K., Kurihara, H., Sugai, M., Susceptibilities of periodontopathogenic and cariogenic bacteria to antibacterial peptides, beta-defensins and LL37, produced by human epithelial cells. J. Antimicrob. Chemother. 55 (2005), 888–896.
    • (2005) J. Antimicrob. Chemother. , vol.55 , pp. 888-896
    • Ouhara, K.1    Komatsuzawa, H.2    Yamada, S.3    Shiba, H.4    Fujiwara, T.5    Ohara, M.6    Sayama, K.7    Hashimoto, K.8    Kurihara, H.9    Sugai, M.10
  • 189
    • 84884389827 scopus 로고    scopus 로고
    • LL-37 opsonizes and inhibits biofilm formation of Aggregatibacter actinomycetemcomitans at subbactericidal concentrations
    • [189] Sol, A., Ginesin, O., Chaushu, S., Karra, L., Coppenhagen-Glazer, S., Ginsburg, I., Bachrach, G., LL-37 opsonizes and inhibits biofilm formation of Aggregatibacter actinomycetemcomitans at subbactericidal concentrations. Infect. Immun. 81 (2013), 3577–3585.
    • (2013) Infect. Immun. , vol.81 , pp. 3577-3585
    • Sol, A.1    Ginesin, O.2    Chaushu, S.3    Karra, L.4    Coppenhagen-Glazer, S.5    Ginsburg, I.6    Bachrach, G.7
  • 190
    • 33748929145 scopus 로고    scopus 로고
    • Antimicrobial activity of an abiotic host defense peptide mimic
    • [190] Tew, G.N., Clements, D., Tang, H., Arnt, L., Scott, R.W., Antimicrobial activity of an abiotic host defense peptide mimic. Biochim. Biophys. Acta 1758 (2006), 1387–1392.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1387-1392
    • Tew, G.N.1    Clements, D.2    Tang, H.3    Arnt, L.4    Scott, R.W.5
  • 191
    • 33749170651 scopus 로고    scopus 로고
    • Effect of MUC7 peptides on the growth of bacteria and on Streptococcus mutans biofilm
    • [191] Wei, G.X., Campagna, A.N., Bobek, L.A., Effect of MUC7 peptides on the growth of bacteria and on Streptococcus mutans biofilm. J. Antimicrob. Chemother. 57 (2006), 1100–1109.
    • (2006) J. Antimicrob. Chemother. , vol.57 , pp. 1100-1109
    • Wei, G.X.1    Campagna, A.N.2    Bobek, L.A.3
  • 193
    • 84862830535 scopus 로고    scopus 로고
    • Effect of a novel antimicrobial peptide chrysophsin-1 on oral pathogens and Streptococcus mutans biofilms
    • [193] Wang, W., Tao, R., Tong, Z., Ding, Y., Kuang, R., Zhai, S., Liu, J., Ni, L., Effect of a novel antimicrobial peptide chrysophsin-1 on oral pathogens and Streptococcus mutans biofilms. Peptides 33 (2012), 212–219.
    • (2012) Peptides , vol.33 , pp. 212-219
    • Wang, W.1    Tao, R.2    Tong, Z.3    Ding, Y.4    Kuang, R.5    Zhai, S.6    Liu, J.7    Ni, L.8
  • 195
    • 0024370068 scopus 로고
    • Purification and characterization of human neutrophil peptide 4, a novel member of the defensin family
    • [195] Wilde, C.G., Griffith, J.E., Marra, M.N., Snable, J.L., Scott, R.W., Purification and characterization of human neutrophil peptide 4, a novel member of the defensin family. J. Biol. Chem. 264 (1989), 11200–11203.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11200-11203
    • Wilde, C.G.1    Griffith, J.E.2    Marra, M.N.3    Snable, J.L.4    Scott, R.W.5
  • 196
    • 63949086432 scopus 로고    scopus 로고
    • Disinfection of maxillofacial silicone elastomer using a novel antimicrobial agent: recombinant human beta-defensin-3
    • [196] Shi, Y., Song, W., Feng, Z.H., Zhao, Y.T., Li, F., Tian, Y., Zhao, Y.M., Disinfection of maxillofacial silicone elastomer using a novel antimicrobial agent: recombinant human beta-defensin-3. Eur. J. Clin. Microbiol. Infect Dis. 28 (2009), 415–420.
    • (2009) Eur. J. Clin. Microbiol. Infect Dis. , vol.28 , pp. 415-420
    • Shi, Y.1    Song, W.2    Feng, Z.H.3    Zhao, Y.T.4    Li, F.5    Tian, Y.6    Zhao, Y.M.7
  • 197
    • 20544447535 scopus 로고    scopus 로고
    • Candidacidal effects of two antimicrobial peptides: histatin 5 causes small membrane defects, but LL-37 causes massive disruption of the cell membrane
    • [197] den Hertog, A.L., van Marle, J., van Veen, H.A., Van't Hof, W., Bolscher, J.G., Veerman, E.C., Nieuw Amerongen, A.V., Candidacidal effects of two antimicrobial peptides: histatin 5 causes small membrane defects, but LL-37 causes massive disruption of the cell membrane. Biochem. J. 388 (2005), 689–695.
    • (2005) Biochem. J. , vol.388 , pp. 689-695
    • den Hertog, A.L.1    van Marle, J.2    van Veen, H.A.3    Van't Hof, W.4    Bolscher, J.G.5    Veerman, E.C.6    Nieuw Amerongen, A.V.7
  • 198
    • 67349118945 scopus 로고    scopus 로고
    • Sensitivity of Candida albicans biofilm cells grown on denture acrylic to antifungal proteins and chlorhexidine
    • [198] Pusateri, C.R., Monaco, E.A., Edgerton, M., Sensitivity of Candida albicans biofilm cells grown on denture acrylic to antifungal proteins and chlorhexidine. Arch. Oral Biol. 54 (2009), 588–594.
    • (2009) Arch. Oral Biol. , vol.54 , pp. 588-594
    • Pusateri, C.R.1    Monaco, E.A.2    Edgerton, M.3
  • 199
    • 79955542011 scopus 로고    scopus 로고
    • Rationale-based, de novo design of dehydrophenylalanine-containing antibiotic peptides and systematic modifi cation in sequence for enhanced potency
    • [199] Pathak, S., Chauhan, V.S., Rationale-based, de novo design of dehydrophenylalanine-containing antibiotic peptides and systematic modifi cation in sequence for enhanced potency. Antimicrob. Agents Chemother. 55 (2011), 2178–2188.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 2178-2188
    • Pathak, S.1    Chauhan, V.S.2
  • 200
    • 84921423477 scopus 로고    scopus 로고
    • Antimicrobial and immunomodulatory properties of PGLa-AM1, CPF-AM1, and magainin-AM1: potent activity against oral pathogens
    • [200] McLean, D.T., McCrudden, M.T., Linden, G.J., Irwin, C.R., Conlon, J.M., Lundy, F.T., Antimicrobial and immunomodulatory properties of PGLa-AM1, CPF-AM1, and magainin-AM1: potent activity against oral pathogens. Regul. Pept. 194–195 (2014), 63–68.
    • (2014) Regul. Pept. , vol.194-195 , pp. 63-68
    • McLean, D.T.1    McCrudden, M.T.2    Linden, G.J.3    Irwin, C.R.4    Conlon, J.M.5    Lundy, F.T.6
  • 201
    • 79955405782 scopus 로고    scopus 로고
    • Antimicrobial decapeptide KSL-W attenuates Candida albicans virulence by modulating its effects on Toll-like receptor, human β-defensin, and cytokine expression by engineered human oral mucosa
    • [201] Semlali, A., Leung, K.P., Curt, S., Rouabhia, M., Antimicrobial decapeptide KSL-W attenuates Candida albicans virulence by modulating its effects on Toll-like receptor, human β-defensin, and cytokine expression by engineered human oral mucosa. Peptides 32 (2011), 859–867.
    • (2011) Peptides , vol.32 , pp. 859-867
    • Semlali, A.1    Leung, K.P.2    Curt, S.3    Rouabhia, M.4
  • 202
    • 84904352945 scopus 로고    scopus 로고
    • C. albicans growth, transition, biofilm formation, and gene expression modulation by antimicrobial decapeptide KSL-W
    • [202] Theberge, S., Semlali, A., Alamri, A., Leung, K.P., Rouabhia, M., C. albicans growth, transition, biofilm formation, and gene expression modulation by antimicrobial decapeptide KSL-W. BMC Microbiol., 13, 2013, 246.
    • (2013) BMC Microbiol. , vol.13 , pp. 246
    • Theberge, S.1    Semlali, A.2    Alamri, A.3    Leung, K.P.4    Rouabhia, M.5
  • 203
    • 84920256643 scopus 로고    scopus 로고
    • Effects of antimicrobial peptide L-K6, a temporin-1CEb analog on oral pathogen growth, Streptococcus mutans biofilm formation, and anti-inflammatory activity
    • [203] Shang, D., Liang, H., Wei, S., Yan, X., Yang, Q., Sun, Y., Effects of antimicrobial peptide L-K6, a temporin-1CEb analog on oral pathogen growth, Streptococcus mutans biofilm formation, and anti-inflammatory activity. Appl. Microbiol. Biotechnol. 98 (2014), 8685–8695.
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 8685-8695
    • Shang, D.1    Liang, H.2    Wei, S.3    Yan, X.4    Yang, Q.5    Sun, Y.6
  • 204
  • 206
    • 80051550773 scopus 로고    scopus 로고
    • Antimicrobial and antibiofilm activity of pleurocidin against cariogenic microorganisms
    • [206] Tao, R., Tong, Z., Lin, Y., Xue, Y., Wang, W., Kuang, R., Wang, P., Tian, Y., Ni, L., Antimicrobial and antibiofilm activity of pleurocidin against cariogenic microorganisms. Peptides 32 (2011), 1748–1754.
    • (2011) Peptides , vol.32 , pp. 1748-1754
    • Tao, R.1    Tong, Z.2    Lin, Y.3    Xue, Y.4    Wang, W.5    Kuang, R.6    Wang, P.7    Tian, Y.8    Ni, L.9
  • 207
    • 1242329995 scopus 로고    scopus 로고
    • In vitro antibacterial activity of the peptide PsVP-10 against antimicrobial-resistant Enterococcus faecalis isolated from clinical samples
    • [207] Padilla, C., Lobos, O., Brevis, P., Abaca, P., Hubert, E., In vitro antibacterial activity of the peptide PsVP-10 against antimicrobial-resistant Enterococcus faecalis isolated from clinical samples. J. Antimicrob. Chemother. 53 (2004), 390–392.
    • (2004) J. Antimicrob. Chemother. , vol.53 , pp. 390-392
    • Padilla, C.1    Lobos, O.2    Brevis, P.3    Abaca, P.4    Hubert, E.5
  • 208
    • 0001475281 scopus 로고    scopus 로고
    • Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction
    • [208] Garcia, J.R., Jaumann, F., Schulz, S., Krause, A., Rodríguez-Jiménez, J., Forssmann, U., Adermann, K., Klüver, E., Vogelmeier, C., Becker, D., Hedrich, R., Forssmann, W.G., Bals, R., Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction. Cell Tissue Res. 306 (2001), 257–264.
    • (2001) Cell Tissue Res. , vol.306 , pp. 257-264
    • Garcia, J.R.1    Jaumann, F.2    Schulz, S.3    Krause, A.4    Rodríguez-Jiménez, J.5    Forssmann, U.6    Adermann, K.7    Klüver, E.8    Vogelmeier, C.9    Becker, D.10    Hedrich, R.11    Forssmann, W.G.12    Bals, R.13
  • 209
    • 84940893101 scopus 로고    scopus 로고
    • Efficacy of a novel antimicrobial peptide against periodontal pathogens in both planktonic and polymicrobial biofilm states
    • [209] Wang, H.Y., Cheng, J.W., Yu, H.Y., Lin, L., Chih, Y.H., Pan, Y.P., Efficacy of a novel antimicrobial peptide against periodontal pathogens in both planktonic and polymicrobial biofilm states. Acta Biomater. 25 (2015), 150–161.
    • (2015) Acta Biomater. , vol.25 , pp. 150-161
    • Wang, H.Y.1    Cheng, J.W.2    Yu, H.Y.3    Lin, L.4    Chih, Y.H.5    Pan, Y.P.6
  • 210
    • 0032821714 scopus 로고    scopus 로고
    • Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens
    • [210] Groenink, J., Walgreen-Weterings, E., van ‘t Hof, W., Veerman, E.C., Nieuw Amerongen, A.V., Cationic amphipathic peptides, derived from bovine and human lactoferrins, with antimicrobial activity against oral pathogens. FEMS Microbiol. Lett. 179 (1999), 217–222.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 217-222
    • Groenink, J.1    Walgreen-Weterings, E.2    van ‘t Hof, W.3    Veerman, E.C.4    Nieuw Amerongen, A.V.5
  • 211
    • 84872019672 scopus 로고    scopus 로고
    • Human neutrophil defensins and their effect on epithelial cells
    • [211] Gursoy, U.K., Kononen, E., Luukkonen, N., Uitto, V.J., Human neutrophil defensins and their effect on epithelial cells. J. Periodontol. 84 (2013), 126–133.
    • (2013) J. Periodontol. , vol.84 , pp. 126-133
    • Gursoy, U.K.1    Kononen, E.2    Luukkonen, N.3    Uitto, V.J.4
  • 212
    • 0034194257 scopus 로고    scopus 로고
    • Large-scale synthesis and functional elements for the antimicrobial activity of defensins
    • [212] Raj, P.A., Antonyraj, K.J., Karunakaran, T., Large-scale synthesis and functional elements for the antimicrobial activity of defensins. Biochem. J. 347 (2000), 633–641.
    • (2000) Biochem. J. , vol.347 , pp. 633-641
    • Raj, P.A.1    Antonyraj, K.J.2    Karunakaran, T.3
  • 213
    • 84939260192 scopus 로고    scopus 로고
    • Novel antimicrobial peptide specifically active against Porphyromonas gingivalis
    • [213] Suwandecha, T., Srichana, T., Balekar, N., Nakpheng, T., Pangsomboon, K., Novel antimicrobial peptide specifically active against Porphyromonas gingivalis. Arch. Microbiol. 197 (2015), 899–909.
    • (2015) Arch. Microbiol. , vol.197 , pp. 899-909
    • Suwandecha, T.1    Srichana, T.2    Balekar, N.3    Nakpheng, T.4    Pangsomboon, K.5
  • 214
    • 35848940745 scopus 로고    scopus 로고
    • Peptide inhibitor of Streptococcus mutans in the control of dental caries
    • [214] Kelly, C.G., Lehner, T., Peptide inhibitor of Streptococcus mutans in the control of dental caries. Int. J. Pept. Res. Ther. 13 (2007), 517–523.
    • (2007) Int. J. Pept. Res. Ther. , vol.13 , pp. 517-523
    • Kelly, C.G.1    Lehner, T.2
  • 215
    • 33750468687 scopus 로고    scopus 로고
    • Host-derived pentapeptide affecting adhesion, proliferation, and local pH in biofilm communities composed of Streptococcus and Actinomyces species
    • [215] Drobni, M., Li, T., Krüger, C., Loimaranta, V., Kilian, M., Hammarström, L., Jörnvall, H., Bergman, T., Strömberg, N., Host-derived pentapeptide affecting adhesion, proliferation, and local pH in biofilm communities composed of Streptococcus and Actinomyces species. Infect. Immun. 74 (2006), 6293–6299.
    • (2006) Infect. Immun. , vol.74 , pp. 6293-6299
    • Drobni, M.1    Li, T.2    Krüger, C.3    Loimaranta, V.4    Kilian, M.5    Hammarström, L.6    Jörnvall, H.7    Bergman, T.8    Strömberg, N.9
  • 216
    • 81255157519 scopus 로고    scopus 로고
    • Impact of the broad-spectrum antimicrobial peptide, lacticin 3147, on Streptococcus mutans growing in a biofilm and in human saliva
    • [216] Dobson, A., O'Connor, P.M., Cotter, P.D., Ross, R.P., Hill, C., Impact of the broad-spectrum antimicrobial peptide, lacticin 3147, on Streptococcus mutans growing in a biofilm and in human saliva. J. Appl. Microbiol. 111 (2011), 1515–1523.
    • (2011) J. Appl. Microbiol. , vol.111 , pp. 1515-1523
    • Dobson, A.1    O'Connor, P.M.2    Cotter, P.D.3    Ross, R.P.4    Hill, C.5
  • 217
    • 33845246336 scopus 로고    scopus 로고
    • Acyl-substituted dermaseptin S4 derivatives with improved bactericidal properties, including on oral microflora
    • [217] Porat, Y., Marynka, K., Tam, A., Steinberg, D., Mor, A., Acyl-substituted dermaseptin S4 derivatives with improved bactericidal properties, including on oral microflora. Antimicrob. Agents Chemother. 50 (2006), 4153–4160.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 4153-4160
    • Porat, Y.1    Marynka, K.2    Tam, A.3    Steinberg, D.4    Mor, A.5
  • 220
    • 35848940309 scopus 로고    scopus 로고
    • Antimicrobial peptides and their potential as oral therapeutic agents
    • [220] Dashper, S.G., Liu, S.W., Reynolds, E.C., Antimicrobial peptides and their potential as oral therapeutic agents. Int. J. Pept. Res. Ther. 13 (2007), 505–516.
    • (2007) Int. J. Pept. Res. Ther. , vol.13 , pp. 505-516
    • Dashper, S.G.1    Liu, S.W.2    Reynolds, E.C.3
  • 221
    • 85009709806 scopus 로고    scopus 로고
    • Antimicrobial effect of an oxazolidinone, lantibiotic and calcium hydroxide against Enterococcus faecalis biofilm: An in vitro study
    • [221] Taneja, S., Kumar, P., Malhotra, K., Dhillon, J., Antimicrobial effect of an oxazolidinone, lantibiotic and calcium hydroxide against Enterococcus faecalis biofilm: An in vitro study. Indian J. Dent. 6 (2015), 190–194.
    • (2015) Indian J. Dent. , vol.6 , pp. 190-194
    • Taneja, S.1    Kumar, P.2    Malhotra, K.3    Dhillon, J.4
  • 222
    • 84959551712 scopus 로고    scopus 로고
    • Birring, To comparatively evaluate the antimicrobial efficacy of chlorhexidine, nisin and linezolid as an intracanal medicament on Enterococcus faecalis: an in vitro study, Indian
    • [222] Somanath, G., Samant, P.S., Gautam, V., Singh, O.J., Birring, To comparatively evaluate the antimicrobial efficacy of chlorhexidine, nisin and linezolid as an intracanal medicament on Enterococcus faecalis: an in vitro study, Indian. J. Dent. Res. 26 (2015), 613–618.
    • (2015) J. Dent. Res. , vol.26 , pp. 613-618
    • Somanath, G.1    Samant, P.S.2    Gautam, V.3    Singh, O.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.