메뉴 건너뛰기




Volumn 105, Issue , 2015, Pages 106-119

Design and studies of multiple mechanism of anti-Candida activity of a new potent Trp-rich peptide dendrimers

Author keywords

Apoptosis; Aspartic protease; Biofilm; Candida; Inhibitor; Necrosis; Synthesis; Trp rich dendrimers

Indexed keywords

ANTIFUNGAL AGENT; ASPARTIC PROTEINASE; FLUORESCEIN; HYDROCARBON; LIPOCORTIN 5; N METHYLTRYPTOPHAN; PHOSPHATIDYLSERINE; PROPIDIUM IODIDE; TRYPTAMINE; TRYPTOPHAN RICH PEPTIDE DENDRIMER; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; DENDRIMER; TRYPTOPHAN;

EID: 84944745102     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2015.10.013     Document Type: Article
Times cited : (35)

References (47)
  • 1
    • 74949107171 scopus 로고    scopus 로고
    • Epidemiology of invasive mycoses in North America
    • M.A. Pfaller, D.J. Diekema, Epidemiology of invasive mycoses in North America, Crit. Rev. Microbiol. 36 (2010) 1-53.
    • (2010) Crit. Rev. Microbiol. , vol.36 , pp. 1-53
    • Pfaller, M.A.1    Diekema, D.J.2
  • 2
    • 84893534198 scopus 로고    scopus 로고
    • Budget impact analysis of liposomal amphotericin B and amphotericin B lipid complex in the treatment of invasive fungal infections in the United States
    • H. Yang, P. Chaudhari, Z.-Y. Zhou, E.Q. Wu, C. Patel, D.L. Horn, Budget impact analysis of liposomal amphotericin B and amphotericin B lipid complex in the treatment of invasive fungal infections in the United States, Appl. Health Econ. Health Policy 12 (2014) 85-93.
    • (2014) Appl. Health Econ. Health Policy , vol.12 , pp. 85-93
    • Yang, H.1    Chaudhari, P.2    Zhou, Z.-Y.3    Wu, E.Q.4    Patel, C.5    Horn, D.L.6
  • 3
    • 77955557244 scopus 로고    scopus 로고
    • Design, synthesis and antifungal activity of isosteric analogues of benzoheterocyclic N-myristoyltransferase inhibitors
    • C. Sheng, H. Xu, W. Wang, et al., Design, synthesis and antifungal activity of isosteric analogues of benzoheterocyclic N-myristoyltransferase inhibitors, Eur. J. Med. Chem. 45 (2010) 3531-3540.
    • (2010) Eur. J. Med. Chem. , vol.45 , pp. 3531-3540
    • Sheng, C.1    Xu, H.2    Wang, W.3
  • 4
    • 84892981925 scopus 로고    scopus 로고
    • Genomic identification of potential targets unique to Candida albicans for the discovery of antifungal agents
    • H. Tripathi, S. Luqman, A. Meena, F. Khan, Genomic identification of potential targets unique to Candida albicans for the discovery of antifungal agents, Curr. Drug Targets 15 (2014) 136-149.
    • (2014) Curr. Drug Targets , vol.15 , pp. 136-149
    • Tripathi, H.1    Luqman, S.2    Meena, A.3    Khan, F.4
  • 5
    • 84929501304 scopus 로고    scopus 로고
    • Inactivation of the antifungal and immunomodulatory properties of human cathelicidin LL-37 by aspartic proteases produced by the pathogenic yeast Candida albicans
    • M. Rapala-Kozik, O. Bochenska, M. Zawrotniak, et al., Inactivation of the antifungal and immunomodulatory properties of human cathelicidin LL-37 by aspartic proteases produced by the pathogenic yeast Candida albicans, Infect. Immun. 83 (2015) 2518-2530.
    • (2015) Infect. Immun. , vol.83 , pp. 2518-2530
    • Rapala-Kozik, M.1    Bochenska, O.2    Zawrotniak, M.3
  • 6
    • 84928176611 scopus 로고    scopus 로고
    • Induction of caspase-11 by aspartyl proteinases of Candida albicans and implication in promoting inflammatory response
    • E. Gabrielli, E. Pericolini, E. Luciano, et al., Induction of caspase-11 by aspartyl proteinases of Candida albicans and implication in promoting inflammatory response, Infect. Immun. 83 (2015) 1940-1948.
    • (2015) Infect. Immun. , vol.83 , pp. 1940-1948
    • Gabrielli, E.1    Pericolini, E.2    Luciano, E.3
  • 7
    • 0141789642 scopus 로고    scopus 로고
    • Candida albicans secreted aspartyl proteinases in virulence and pathogenesis
    • J.R. Naglik, S.J. Challacombe, B. Hube, Candida albicans secreted aspartyl proteinases in virulence and pathogenesis, Microbiol. Mol. Biol. Rev. 67 (2003) 400-428.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 400-428
    • Naglik, J.R.1    Challacombe, S.J.2    Hube, B.3
  • 8
    • 27244436568 scopus 로고    scopus 로고
    • Contributions of hyphae and hypha-co-regulated genes to Candida albicans virulence
    • C.A. Kumamoto, M.D. Vinces, Contributions of hyphae and hypha-co-regulated genes to Candida albicans virulence, Cell Microbiol. 7 (2005) 1546-1554.
    • (2005) Cell Microbiol , vol.7 , pp. 1546-1554
    • Kumamoto, C.A.1    Vinces, M.D.2
  • 9
    • 0036854439 scopus 로고    scopus 로고
    • Differential secretion of Sap4-6 proteins in Candida albicans during hyphae formation
    • Y.C. Chen, C.C. Wu, W.L. Chung, F.J. Lee, Differential secretion of Sap4-6 proteins in Candida albicans during hyphae formation, Microbiology 148 (2002) 3743-3754.
    • (2002) Microbiology , vol.148 , pp. 3743-3754
    • Chen, Y.C.1    Wu, C.C.2    Chung, W.L.3    Lee, F.J.4
  • 10
    • 0032722557 scopus 로고    scopus 로고
    • Misexpression of the opaque-phase-specific gene PEP1 (SAP1) in the white phase of Candida albicans confers increased virulence in a mouse model of cutaneous infection
    • C.S. Kvaal, S.A. Lachke, T. Srikantha, K. Daniels, J. McCoy, D.R. Soll, Misexpression of the opaque-phase-specific gene PEP1 (SAP1) in the white phase of Candida albicans confers increased virulence in a mouse model of cutaneous infection, Infect. Immun. 67 (1999) 6652-6662.
    • (1999) Infect. Immun. , vol.67 , pp. 6652-6662
    • Kvaal, C.S.1    Lachke, S.A.2    Srikantha, T.3    Daniels, K.4    McCoy, J.5    Soll, D.R.6
  • 11
    • 84877994942 scopus 로고    scopus 로고
    • Human serum promotes Candida albicans biofilm growth and virulence gene expression on silicone biomaterial
    • Y.H. Samaranayake, B.P. Cheung, J.Y. Yau, S.K. Yeung, L.P. Samaranayake, Human serum promotes Candida albicans biofilm growth and virulence gene expression on silicone biomaterial, PLoS One 8 (2013) e62902, http://dx.doi.org/10.1371/journal.pone.0062902.
    • (2013) PLoS One , vol.8 , pp. e62902
    • Samaranayake, Y.H.1    Cheung, B.P.2    Yau, J.Y.3    Yeung, S.K.4    Samaranayake, L.P.5
  • 12
    • 84883004752 scopus 로고    scopus 로고
    • Candidiasis drug discovery and development: New approaches targeting virulence for discovering and identifying new drugs
    • C.G. Pierce, J.L. Lopez-Ribot, Candidiasis drug discovery and development: new approaches targeting virulence for discovering and identifying new drugs, Expert Opin. Drug Discov. 8 (2013) 11117-11126.
    • (2013) Expert Opin. Drug Discov. , vol.8 , pp. 11117-11126
    • Pierce, C.G.1    Lopez-Ribot, J.L.2
  • 13
    • 0344630224 scopus 로고    scopus 로고
    • Apoptosis induced by environmental stresses and amphotericin B in Candida albicans
    • A.J. Phillips, I. Sudbery, M. Ramsdale, Apoptosis induced by environmental stresses and amphotericin B in Candida albicans, PNAS 100 (2003) 14327-14332.
    • (2003) PNAS , vol.100 , pp. 14327-14332
    • Phillips, A.J.1    Sudbery, I.2    Ramsdale, M.3
  • 14
    • 58149187882 scopus 로고    scopus 로고
    • APD2: The updated antimicrobial peptide database and its application in peptide design
    • G. Wang, X. Li, Z. Wang, APD2: the updated antimicrobial peptide database and its application in peptide design, Nucleic Acids Res. 37 (2009) D933eD937.
    • (2009) Nucleic Acids Res , vol.37 , pp. D933eD937
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 15
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the Nterminal region of bovine lactoferrin
    • W. Bellamy, M. Takase, H. Wakabayashi, K. Kawase, M. Tomita, Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the Nterminal region of bovine lactoferrin, J. Appl. Bacteriol. 73 (1992) 472-479.
    • (1992) J. Appl. Bacteriol. , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5
  • 17
    • 0030586288 scopus 로고    scopus 로고
    • Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides
    • C. Lawyer, S. Pai, M. Watabe, et al., Antimicrobial activity of a 13 amino acid tryptophan-rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptides, FEBS Lett. 390 (1996) 95-98.
    • (1996) FEBS Lett , vol.390 , pp. 95-98
    • Lawyer, C.1    Pai, S.2    Watabe, M.3
  • 18
    • 84903547359 scopus 로고    scopus 로고
    • The in vitro effects of new D186 dendrimer on virulence factors of Candida albicans
    • M. Staniszewska, M. Bondaryk, P. Zieli-nska, Z. Urba-nczyk-Lipkowska, The in vitro effects of new D186 dendrimer on virulence factors of Candida albicans, J. Antibiot. 67 (2014) 425-432.
    • (2014) J. Antibiot. , vol.67 , pp. 425-432
    • Staniszewska, M.1    Bondaryk, M.2    Zielinska, P.3    Urbanczyk-Lipkowska, Z.4
  • 19
    • 0028340489 scopus 로고
    • Selection of candidate quality control isolates and tentative quality control ranges for in vitro susceptibility testing of yeast isolates by National Committee for Clinical Laboratory Standards proposed standard methods
    • M.A. Pfaller, M. Bale, B. Buschelman, et al., Selection of candidate quality control isolates and tentative quality control ranges for in vitro susceptibility testing of yeast isolates by National Committee for Clinical Laboratory Standards proposed standard methods, J. Clin. Microbiol. 32 (1994) 1650-1653.
    • (1994) J. Clin. Microbiol. , vol.32 , pp. 1650-1653
    • Pfaller, M.A.1    Bale, M.2    Buschelman, B.3
  • 20
    • 57349131646 scopus 로고    scopus 로고
    • Secreted aspartic proteases are not require for invasion of reconstituted human epithelia by Candida albicans
    • U. Lermann, J. Morschhauser, Secreted aspartic proteases are not require for invasion of reconstituted human epithelia by Candida albicans, Microbiology 154 (2008) 3281-3295.
    • (2008) Microbiology , vol.154 , pp. 3281-3295
    • Lermann, U.1    Morschhauser, J.2
  • 21
    • 37849041277 scopus 로고    scopus 로고
    • Tetracycline-inducible expression of individual secreted aspartic proteases in Candida albicans allows isoenzyme-specific inhibitor screening
    • P. Staib, U. Lermann, J. Blaß-Warmuth, et al., Tetracycline-inducible expression of individual secreted aspartic proteases in Candida albicans allows isoenzyme-specific inhibitor screening, Antimicrob. Agents Chemother. 52 (2008) 146-156.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 146-156
    • Staib, P.1    Lermann, U.2    Blaß-Warmuth, J.3
  • 22
    • 0033051961 scopus 로고    scopus 로고
    • Identification of CARE-2-negative Candida albicans isolates as Candida dubliniensis
    • J. Morschhauser, M. Ruhnke, S. Michel, J. Hacker, Identification of CARE-2-negative Candida albicans isolates as Candida dubliniensis, Mycoses 42 (1999) 29-32.
    • (1999) Mycoses , vol.42 , pp. 29-32
    • Morschhauser, J.1    Ruhnke, M.2    Michel, S.3    Hacker, J.4
  • 23
    • 0342930292 scopus 로고
    • Note on the importance of hyphomycetes and other fungi in tropical pathology
    • A. Castellani, Note on the importance of hyphomycetes and other fungi in tropical pathology, Br. Med. J. 2 (1912) 1208-1212.
    • (1912) Br. Med. J. , vol.2 , pp. 1208-1212
    • Castellani, A.1
  • 24
    • 0010556667 scopus 로고
    • Certain conditions of the gastro-intestinal tract in Porto Rico and their relation to tropical sprue
    • B.K. Ashford, Certain conditions of the gastro-intestinal tract in Porto Rico and their relation to tropical sprue, Am. J. Trop. Med. Hyg. 8 (1928) 507-538.
    • (1928) Am. J. Trop. Med. Hyg. , vol.8 , pp. 507-538
    • Ashford, B.K.1
  • 26
    • 78449238453 scopus 로고    scopus 로고
    • The Candida albicans Rgd1 is a RhoGAP protein involved in the control of filamentous growth
    • F. Ness, V. Prouzet-Mauleon, A. Vieillemard, et al., The Candida albicans Rgd1 is a RhoGAP protein involved in the control of filamentous growth, Fungal Genet. Biol. 47 (2010) 1001-1011.
    • (2010) Fungal Genet. Biol. , vol.47 , pp. 1001-1011
    • Ness, F.1    Prouzet-Mauleon, V.2    Vieillemard, A.3
  • 27
    • 72049105042 scopus 로고    scopus 로고
    • New small-size peptides possessing antifungal activity
    • F.M. Garibotto, A.D. Garro, M.F. Masman, et al., New small-size peptides possessing antifungal activity, Bioorg. Med. Chem. 18 (2010) 158-167.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 158-167
    • Garibotto, F.M.1    Garro, A.D.2    Masman, M.F.3
  • 28
    • 23044477789 scopus 로고    scopus 로고
    • Capsofungin susceptibility testing of Candida inconspicua: Correlation of different methods with the minimal fungicidal concentration
    • L. Majoros, G. Kardos, B. Szab-o, M. Sipiczki, Capsofungin susceptibility testing of Candida inconspicua: correlation of different methods with the minimal fungicidal concentration, Antimicrob. Agents Chemother. 49 (2005) 3486-3488.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3486-3488
    • Majoros, L.1    Kardos, G.2    Szabo, B.3    Sipiczki, M.4
  • 29
    • 33749017739 scopus 로고    scopus 로고
    • Differences in amphotericin B-induced hemolysis between human erythrocytes obtained from male and female donors
    • A. Knopik-Skrocka, J. Bielawski, Differences in amphotericin B-induced hemolysis between human erythrocytes obtained from male and female donors, Biol. Lett. 42 (2005) 49-60.
    • (2005) Biol. Lett. , vol.42 , pp. 49-60
    • Knopik-Skrocka, A.1    Bielawski, J.2
  • 30
    • 84872029205 scopus 로고    scopus 로고
    • Capsofungin kills Candida albicans by causing both cellular apoptosis and necrosis
    • B. Hao, S. Cheng, C.J. Clancy, M.H. Nguyen, Capsofungin kills Candida albicans by causing both cellular apoptosis and necrosis, Antimicrob. Agents Chemother. 57 (2013) 326-332.
    • (2013) Antimicrob. Agents Chemother. , vol.57 , pp. 326-332
    • Hao, B.1    Cheng, S.2    Clancy, C.J.3    Nguyen, M.H.4
  • 31
    • 84921523986 scopus 로고    scopus 로고
    • On the antimicrobial activity of various peptide-based dendrimers of similar architecture
    • T.K. Lind, P. Polcyn, P. Zielinska, M. Cardenas, Z. Urbanczyk-Lipkowska, On the antimicrobial activity of various peptide-based dendrimers of similar architecture, Molecules 20 (2015) 738-753.
    • (2015) Molecules , vol.20 , pp. 738-753
    • Lind, T.K.1    Polcyn, P.2    Zielinska, P.3    Cardenas, M.4    Urbanczyk-Lipkowska, Z.5
  • 32
    • 84891305354 scopus 로고    scopus 로고
    • Reactive oxygen species-inducing antifungal agents and their activity against fungal biofilms
    • N. Delattin, B.P. Cammue, K. Thevissen, Reactive oxygen species-inducing antifungal agents and their activity against fungal biofilms, Future Med. Chem. 6 (2014) 77-90.
    • (2014) Future Med. Chem. , vol.6 , pp. 77-90
    • Delattin, N.1    Cammue, B.P.2    Thevissen, K.3
  • 33
    • 46549083882 scopus 로고    scopus 로고
    • Programmed cell death in pathogenic fungi
    • M. Ramsdale, Programmed cell death in pathogenic fungi, Biochim. Biophys. Acta 1783 (2008) 1369-1380.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1369-1380
    • Ramsdale, M.1
  • 34
    • 84888046119 scopus 로고    scopus 로고
    • Design of short membrane selective antimicrobial peptides containing tryptophan and arginine residues for improved activity, salt-resistance, and biocompatibility
    • R. Saravanan, X. Li, K. Lim, et al., Design of short membrane selective antimicrobial peptides containing tryptophan and arginine residues for improved activity, salt-resistance, and biocompatibility, Biotechnol. Bioeng. 111 (2014) 37-49.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 37-49
    • Saravanan, R.1    Li, X.2    Lim, K.3
  • 35
    • 77949825060 scopus 로고    scopus 로고
    • The effects of tryptophan and hydrophobicity on the structure and bioactivity of novel indolicidin with promising pharmaceutical potential
    • A.P. Podorieszach, H.E.K. Huttunen-Hennelly, The effects of tryptophan and hydrophobicity on the structure and bioactivity of novel indolicidin with promising pharmaceutical potential, Org. Biomol. Chem. 8 (2010) 1679-1687.
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 1679-1687
    • Podorieszach, A.P.1    Huttunen-Hennelly, H.E.K.2
  • 36
    • 84896488395 scopus 로고    scopus 로고
    • Echinocandins in the treatment of candidaemia and invasive candidiasis: Clinical and economic perspectives
    • C.F. Neoh, M. Slavin, S.C.A. Chen, K. Stewart, D.C.M. Kong, Echinocandins in the treatment of candidaemia and invasive candidiasis: clinical and economic perspectives, Int. J. Antimicrob. Agents 43 (2014) 207-214.
    • (2014) Int. J. Antimicrob. Agents , vol.43 , pp. 207-214
    • Neoh, C.F.1    Slavin, M.2    Chen, S.C.A.3    Stewart, K.4    Kong, D.C.M.5
  • 37
    • 84919800402 scopus 로고    scopus 로고
    • PAMAM dendrimers: Destined for success or doomed to fail Plain and modified PAMAM dendrimers in the context of biomedical applications
    • M. Labieniec-Watala, C. Watala, PAMAM dendrimers: destined for success or doomed to fail Plain and modified PAMAM dendrimers in the context of biomedical applications, J. Pharm. Sci. 104 (2015) 2-14.
    • (2015) J. Pharm. Sci. , vol.104 , pp. 2-14
    • Labieniec-Watala, M.1    Watala, C.2
  • 38
    • 80053373919 scopus 로고    scopus 로고
    • Apoptosis-inducing antifungal peptides and proteins
    • K. De Brucker, B.P.A. Cammue, K. Thevissen, Apoptosis-inducing antifungal peptides and proteins, Biochem. Soc. T 39 (2011) 1527-1532.
    • (2011) Biochem. Soc. T , vol.39 , pp. 1527-1532
    • De Brucker, K.1    Cammue, B.P.A.2    Thevissen, K.3
  • 40
    • 84922531223 scopus 로고    scopus 로고
    • Susceptibility of Candida albicans to new synthetic sulfone derivatives
    • M. Staniszewska, M. Bondaryk, Z. Ochal, Susceptibility of Candida albicans to new synthetic sulfone derivatives, Arch. Pharm. Chem. Life Sci. 348 (2015) 1-13.
    • (2015) Arch. Pharm. Chem. Life Sci. , vol.348 , pp. 1-13
    • Staniszewska, M.1    Bondaryk, M.2    Ochal, Z.3
  • 41
    • 84891357611 scopus 로고    scopus 로고
    • Sap6, a secreted aspartyl proteinase, participates in maintenance the cell surface integrity of Candida albicans
    • L.M. Buu, Y.C. Chen, Sap6, a secreted aspartyl proteinase, participates in maintenance the cell surface integrity of Candida albicans, J. Biomed. Sci. 20 (2013) 101, http://dx.doi.org/10.1186/1423-0127-20-101.
    • (2013) J. Biomed. Sci. , vol.20 , pp. 101
    • Buu, L.M.1    Chen, Y.C.2
  • 42
    • 84882808925 scopus 로고    scopus 로고
    • Characterization of antimicrobial peptides toward the development of novel antibiotics
    • W. Aoki, M. Ueda, Characterization of antimicrobial peptides toward the development of novel antibiotics, Pharmaceuticals 6 (2013) 1055-1081.
    • (2013) Pharmaceuticals , vol.6 , pp. 1055-1081
    • Aoki, W.1    Ueda, M.2
  • 43
    • 76049117463 scopus 로고    scopus 로고
    • Apoptosis in Candida biofilms exposed to amphotericin B
    • R.S. Al-Dhaheri, J. Douglas, Apoptosis in Candida biofilms exposed to amphotericin B, J. Med. Microbiol. 59 (2010) 149-157.
    • (2010) J. Med. Microbiol. , vol.59 , pp. 149-157
    • Al-Dhaheri, R.S.1    Douglas, J.2
  • 45
    • 84893723955 scopus 로고    scopus 로고
    • Anti-Candida activity of two-peptide bacteriocins, plantaricins (Pln E/F and J/K) and their mode of action
    • A. Sharma, S. Srivastava, Anti-Candida activity of two-peptide bacteriocins, plantaricins (Pln E/F and J/K) and their mode of action, Fungal Biol. 118 (2014) 254-275.
    • (2014) Fungal Biol , vol.118 , pp. 254-275
    • Sharma, A.1    Srivastava, S.2
  • 46
    • 0034791287 scopus 로고    scopus 로고
    • The KEX2 gene Candida glabrata is required for cell surface integrity
    • O. Bader, M. Schaller, S. Klein, et al., The KEX2 gene Candida glabrata is required for cell surface integrity, Mol. Microbiol. 41 (2001) 1431-1444.
    • (2001) Mol. Microbiol. , vol.41 , pp. 1431-1444
    • Bader, O.1    Schaller, M.2    Klein, S.3
  • 47
    • 77953621452 scopus 로고    scopus 로고
    • Transcriptional response to fluconazole and amphotericin B in Candida albicans biofilms
    • H. Nails, D. Vandenbosch, D. Deforce, H.J. Nelis, T. Coenye, Transcriptional response to fluconazole and amphotericin B in Candida albicans biofilms, Res. Microbiol. 161 (2010) 284-292.
    • (2010) Res. Microbiol. , vol.161 , pp. 284-292
    • Nails, H.1    Vandenbosch, D.2    Deforce, D.3    Nelis, H.J.4    Coenye, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.