메뉴 건너뛰기




Volumn 6, Issue 6, 2013, Pages 728-758

Database-guided discovery of potent peptides to combat HIV-1 or superbugs

Author keywords

Ab initio design; Antimicrobial peptides; Biofilms; Database screening; De novo design; HIV 1; Improved 2D NMR method; MRSA; Superbugs; Template based design

Indexed keywords

ALPHA DEFENSIN 1; ANTIBIOTIC AGENT; ANTIINFECTIVE AGENT; ANTIMICROBIAL PEPTIDE BI 32169; ANTIMICROBIAL PEPTIDE GLK 19; ANTIMICROBIAL PEPTIDE GLRC 1; ANTIMICROBIAL PEPTIDE GLRC 2; ANTIMICROBIAL PEPTIDE GLRC 3; ANTIMICROBIAL PEPTIDE GLRC 4; ANTIMICROBIAL PEPTIDE MGD 1; ANTIVIRUS AGENT; AUREIN 1.2; BETA DEFENSIN 1; CAENOPORE 5; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; DISTINCTIN; INDOLICIDIN; KALATA B1; PLECTASIN; POLYPEPTIDE ANTIBIOTIC AGENT; THETA DEFENSIN 1; UNCLASSIFIED DRUG;

EID: 84878419915     PISSN: None     EISSN: 14248247     Source Type: Journal    
DOI: 10.3390/ph6060728     Document Type: Article
Times cited : (90)

References (160)
  • 1
    • 84878409435 scopus 로고    scopus 로고
    • Available online:, accessed on 2 May
    • Alexander Fleming (1881-1955): A Noble Life in Science. Available online: http://www.bl.uk/onlinegallery/features/beautifulminds/fleming.html/ (accessed on 2 May 2013).
    • (2013) Alexander Fleming (1881-1955): A Noble Life In Science
  • 2
    • 85024321592 scopus 로고
    • Studies on a bactericidal agent extracted from a soil bacillus: I. Preparation of the agent. Its activity in vitro
    • Dubos, R.J. Studies on a bactericidal agent extracted from a soil bacillus: I. Preparation of the agent. Its activity in vitro. J. Exp. Med. 1939, 70, 1-10.
    • (1939) J. Exp. Med , vol.70 , pp. 1-10
    • Dubos, R.J.1
  • 3
    • 0015723952 scopus 로고
    • On the effect of a polypeptide isolated from "Kalata-Kalata" (Oldenlandia affinis DC) on the oestrogen dominated uterus
    • Gran, L. On the effect of a polypeptide isolated from "Kalata-Kalata" (Oldenlandia affinis DC) on the oestrogen dominated uterus. Acta Pharmacol. Toxicol. (Copenh) 1973, 33, 400-408.
    • (1973) Acta Pharmacol. Toxicol. (Copenh) , vol.33 , pp. 400-408
    • Gran, L.1
  • 4
    • 0033529942 scopus 로고    scopus 로고
    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides
    • Tam, J.P.; Lu, Y.A.; Yang, J.L.; Chiu, K.W. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. Proc. Natl. Acad. Sci. USA. 1999, 96, 8913-8918.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8913-8918
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3    Chiu, K.W.4
  • 5
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner, H.; Hultmark, D.; Engström, Å.; Bennich, H.; Boman, H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 1981, 292, 246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engström, A.3    Bennich, H.4    Boman, H.G.5
  • 7
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. USA 1987, 84, 5449-5453.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5449-5453
    • Zasloff, M.1
  • 8
    • 0347755460 scopus 로고    scopus 로고
    • The antimicrobial peptide database
    • Wang, Z.; Wang, G. APD: The antimicrobial peptide database. Nucleic Acids Res. 2004, 32, D590-D592.
    • (2004) Nucleic Acids Res , vol.32
    • Wang, Z.1    Wang, G.A.P.D.2
  • 9
    • 58149187882 scopus 로고    scopus 로고
    • The updated antimicrobial peptide database and its application in peptide design
    • Wang, G.; Li, X.; Wang, Z. The updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009, 37, D933-D937.
    • (2009) Nucleic Acids Res , vol.37
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 13
    • 84878420971 scopus 로고    scopus 로고
    • Antiinfective peptides laboratory Tossi group. Available online, accessed on 3 May
    • Antiinfective peptides laboratory Tossi group. Available online: http://www.bbcm.univ.trieste.it/~tossi/amsdb.html (accessed on 3 May 2013).
    • (2013)
  • 14
    • 0346494756 scopus 로고    scopus 로고
    • The Peptaibol Database: A database for sequences and structures of naturally occurring peptaibols
    • Whitmore, L.; Wallace, B.A. The Peptaibol Database: A database for sequences and structures of naturally occurring peptaibols. Nucleic Acids Res. 2004, 32, D593-D594.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 19
    • 77249117208 scopus 로고    scopus 로고
    • BACTIBASE second release: A database and tool platform for bacteriocin characterization
    • Hammami, R.; Zouhir, A.; Le Lay, C.; Ben Hamida, J.; Fliss, I. BACTIBASE second release: A database and tool platform for bacteriocin characterization. BMC Microbiol. 2010, 10, 22.
    • (2010) BMC Microbiol , vol.10 , pp. 22
    • Hammami, R.1    Zouhir, A.2    Le Lay, C.3    Ben Hamida, J.4    Fliss, I.5
  • 20
    • 84866676209 scopus 로고    scopus 로고
    • ThioFinder: A web-based tool for the identification of thiopeptide gene clusters in DNA sequences
    • Li, J.; Qu, X.; He, X.; Duan, L.; Wu, G.; Bi, D.; Deng, Z.; Liu, W.; Ou, H.Y. ThioFinder: A web-based tool for the identification of thiopeptide gene clusters in DNA sequences. PLoS One 2012, 7, e45878.
    • (2012) PLoS One , vol.7
    • Li, J.1    Qu, X.2    He, X.3    Duan, L.4    Wu, G.5    Bi, D.6    Deng, Z.7    Liu, W.8    Ou, H.Y.9
  • 21
    • 38549134937 scopus 로고    scopus 로고
    • CyBase: A database of cyclic protein sequences and structures, with applications in protein discovery and engineering
    • Wang, C.K.; Kaas, Q.; Chiche, L.; Craik, D.J. CyBase: A database of cyclic protein sequences and structures, with applications in protein discovery and engineering. Nucleic Acids Res. 2008, 36, D206-D210.
    • (2008) Nucleic Acids Res , vol.36
    • Wang, C.K.1    Kaas, Q.2    Chiche, L.3    Craik, D.J.4
  • 22
    • 33846108632 scopus 로고    scopus 로고
    • Defensins knowledgebase: A manually curated database and information source focused on the defensins family of antimicrobial peptides
    • Seebah, S.; Suresh, A.; Zhuo, S.; Choong, Y.H.; Chua, H.; Chuon, D.; Beuerman, R.; Verma, C. Defensins knowledgebase: A manually curated database and information source focused on the defensins family of antimicrobial peptides. Nucleic Acids Res. 2007, 35, D265-D268.
    • (2007) Nucleic Acids Res , vol.35
    • Seebah, S.1    Suresh, A.2    Zhuo, S.3    Choong, Y.H.4    Chua, H.5    Chuon, D.6    Beuerman, R.7    Verma, C.8
  • 23
    • 84859512521 scopus 로고    scopus 로고
    • EnzyBase: A novel database for enzybiotic studies
    • Wu, H.; Lu, H.; Huang, J.; Li, G.; Huang, Q. EnzyBase: A novel database for enzybiotic studies. BMC Microbiol. 2012, 12, 54.
    • (2012) BMC Microbiol , vol.12 , pp. 54
    • Wu, H.1    Lu, H.2    Huang, J.3    Li, G.4    Huang, Q.5
  • 24
    • 0036220024 scopus 로고    scopus 로고
    • Synthetic antibiotic peptides database
    • Wade, D.; Englund, J. Synthetic antibiotic peptides database. Protein Pept. Lett. 2002, 9, 53-57.
    • (2002) Protein Pept. Lett , vol.9 , pp. 53-57
    • Wade, D.1    Englund, J.2
  • 25
    • 56649106249 scopus 로고    scopus 로고
    • RAPD: A database of recombinantly-produced antimicrobial peptides
    • Li, Y.; Chen, Z. RAPD: A database of recombinantly-produced antimicrobial peptides. FEMS Microbiol. Lett. 2008, 289, 126-129.
    • (2008) FEMS Microbiol. Lett , vol.289 , pp. 126-129
    • Li, Y.1    Chen, Z.2
  • 26
    • 84877288702 scopus 로고    scopus 로고
    • A database view of natural antimicrobial peptides: Nomenclature, classification and amino acid sequence analysis
    • Wang, G., Ed.; CABI: Wallingford, England
    • Wang, G.; Li, X.; Zasloff, M. A database view of natural antimicrobial peptides: Nomenclature, classification and amino acid sequence analysis. In Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies; Wang, G., Ed.; CABI: Wallingford, England, 2010; pp. 1-21.
    • (2010) Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies , pp. 1-21
    • Wang, G.1    Li, X.2    Zasloff, M.3
  • 27
    • 72049089561 scopus 로고    scopus 로고
    • Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata
    • Ma, Y.; Liu, C.; Liu, X.; Wu, J.; Yang, H.; Wang, Y.; Li, J.; Yu, H.; Lai, R. Peptidomics and genomics analysis of novel antimicrobial peptides from the frog, Rana nigrovittata. Genomics 2010, 95, 66-71.
    • (2010) Genomics , vol.95 , pp. 66-71
    • Ma, Y.1    Liu, C.2    Liu, X.3    Wu, J.4    Yang, H.5    Wang, Y.6    Li, J.7    Yu, H.8    Lai, R.9
  • 28
    • 84862907759 scopus 로고    scopus 로고
    • Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs
    • Yang, X.; Lee, W.H.; Zhang, Y. Extremely Abundant Antimicrobial Peptides Existed in the Skins of Nine Kinds of Chinese Odorous Frogs. J. Proteome Res. 2012, 11, 306-319.
    • (2012) J. Proteome Res , vol.11 , pp. 306-319
    • Yang, X.1    Lee, W.H.2    Zhang, Y.3
  • 29
    • 79960945084 scopus 로고    scopus 로고
    • Structural diversity and species distribution of host-defense peptides in frog skin secretions
    • Conlon, J.M. Structural diversity and species distribution of host-defense peptides in frog skin secretions. Cell. Mol. Life Sci. 2011, 68, 2303-2315.
    • (2011) Cell. Mol. Life Sci , vol.68 , pp. 2303-2315
    • Conlon, J.M.1
  • 30
    • 67649408946 scopus 로고    scopus 로고
    • Bombinins, antimicrobial peptides from Bombina species
    • Simmaco, M.; Kreil, G.; Barra, D. Bombinins, antimicrobial peptides from Bombina species. Biochim. Biophys. Acta 2009, 1788, 1551-1555.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1551-1555
    • Simmaco, M.1    Kreil, G.2    Barra, D.3
  • 31
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellullar organisms
    • Zasloff, M. Antimicrobial peptides of multicellullar organisms. Nature 2002, 415, 359-365.
    • (2002) Nature , vol.415 , pp. 359-365
    • Zasloff, M.1
  • 32
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Tang, Y.Q.; Yuan, J.; Osapay, G.; Osapay, K.; Tran, D.; Miller, C.J.; Ouellette, A.J.; Selsted, M.E. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 1999, 286, 498-502.
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3    Osapay, K.4    Tran, D.5    Miller, C.J.6    Ouellette, A.J.7    Selsted, M.E.8
  • 36
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: Basic facts and emerging concepts
    • Boman, H.G. Antibacterial peptides: Basic facts and emerging concepts. J. Inter. Med. 2003, 254, 197-215.
    • (2003) J. Inter. Med , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 37
    • 84858064379 scopus 로고    scopus 로고
    • Fine tuning host responses in the face of infection: Emerging roles and clinical applications of host defense peptides
    • Wang, G.; Ed.; CABI: Wallingford, England
    • Mayer, M.L.; Easton, D.M.; Hancock, R.E.W. Fine tuning host responses in the face of infection: Emerging roles and clinical applications of host defense peptides. Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies; Wang, G.; Ed.; CABI: Wallingford, England, 2010; pp. 195-220.
    • (2010) Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies , pp. 195-220
    • Mayer, M.L.1    Easton, D.M.2    Hancock, R.E.W.3
  • 38
    • 34047268684 scopus 로고    scopus 로고
    • The host defense of Drosophila melanogaster
    • Lemaitre, B.; Hoffmann, J. The host defense of Drosophila melanogaster. Annu. Rev. Immunol. 2007, 25, 697-743.
    • (2007) Annu. Rev. Immunol , vol.25 , pp. 697-743
    • Lemaitre, B.1    Hoffmann, J.2
  • 39
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov, R.; Preston-Hurlburt, P.; Janeway, C.A., Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997, 388, 394-397.
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 41
    • 84878389919 scopus 로고    scopus 로고
    • Natural antimicrobial peptides as promising anti-HIV candidates
    • Wang, G. Natural antimicrobial peptides as promising anti-HIV candidates. Curr. Topics Pept. Protein Res. 2012, 13, 93-110.
    • (2012) Curr. Topics Pept. Protein Res , vol.13 , pp. 93-110
    • Wang, G.1
  • 42
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock, R.E.W.; Sahl, H.G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 2006, 24, 1551-1557.
    • (2006) Nat. Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.W.1    Sahl, H.G.2
  • 43
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense
    • Lai, Y.; Gallo, R.L. AMPed up immunity: How antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 2009, 30, 131-141.
    • (2009) Trends Immunol , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 44
    • 84874210228 scopus 로고    scopus 로고
    • The importance of amino acid composition in natural AMPs: An evolutional, structural, and functional perspective
    • Mishra, B.; Wang, G. The importance of amino acid composition in natural AMPs: An evolutional, structural, and functional perspective. Frontier Immunol. 2012, 3, 221.
    • (2012) Frontier Immunol , vol.3 , pp. 221
    • Mishra, B.1    Wang, G.2
  • 45
    • 60749130267 scopus 로고    scopus 로고
    • Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs
    • Cherkasov, A.; Hilpert, K.; Jenssen, H.; Fjell, C.D.; Waldbrook, M.; Mullaly, S.C.; Volkmer, R.; Hancock, R.E. Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs. ACS Chem. Biol. 2009, 4, 65-74.
    • (2009) ACS Chem. Biol , vol.4 , pp. 65-74
    • Cherkasov, A.1    Hilpert, K.2    Jenssen, H.3    Fjell, C.D.4    Waldbrook, M.5    Mullaly, S.C.6    Volkmer, R.7    Hancock, R.E.8
  • 46
    • 79954616130 scopus 로고    scopus 로고
    • Prediction of antimicrobial peptides based on sequence alignment and feature selection methods
    • Wang, P.; Hu, L.; Liu, G.; Jiang, N.; Chen, X.; Xu, J.; Zheng, W.; Li, L.; Tan, M.; Chen, Z., et al. Prediction of antimicrobial peptides based on sequence alignment and feature selection methods. PLoS One 2011, 6, e18476.
    • (2011) PLoS One , vol.6
    • Wang, P.1    Hu, L.2    Liu, G.3    Jiang, N.4    Chen, X.5    Xu, J.6    Zheng, W.7    Li, L.8    Tan, M.9    Chen, Z.10
  • 48
    • 34548637974 scopus 로고    scopus 로고
    • Curvature-dependent recognition of ethanolamine phospholipids by duramycin and cinnamycin
    • Iwamoto, K.; Hayakawa, T.; Murate, M.; Makino, A.; Ito, K.; Fujisawa, T.; Kobayashi, T. Curvature-dependent recognition of ethanolamine phospholipids by duramycin and cinnamycin. Biophys. J. 2007, 93, 1608-1619.
    • (2007) Biophys. J , vol.93 , pp. 1608-1619
    • Iwamoto, K.1    Hayakawa, T.2    Murate, M.3    Makino, A.4    Ito, K.5    Fujisawa, T.6    Kobayashi, T.7
  • 49
    • 84855230886 scopus 로고    scopus 로고
    • Lantibiotics as probes for phosphatidylethanolamine
    • Zhao, M. Lantibiotics as probes for phosphatidylethanolamine. Amino Acids 2011, 41, 1071-1079.
    • (2011) Amino Acids , vol.41 , pp. 1071-1079
    • Zhao, M.1
  • 50
    • 14044268292 scopus 로고    scopus 로고
    • Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a non-toxic bacterial membrane anchor
    • Wang, G.; Li, Y.; Li, X. Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a non-toxic bacterial membrane anchor. J. Biol. Chem. 2005, 280, 5803-5811.
    • (2005) J. Biol. Chem , vol.280 , pp. 5803-5811
    • Wang, G.1    Li, Y.2    Li, X.3
  • 51
    • 33750304297 scopus 로고    scopus 로고
    • A linguistic model for the rational design of antimicrobial peptides
    • Loose, C.; Jensen, K.; Rigoutsos, I.; Stephanopoulos, G. A linguistic model for the rational design of antimicrobial peptides. Nature 2006, 443, 867-869.
    • (2006) Nature , vol.443 , pp. 867-869
    • Loose, C.1    Jensen, K.2    Rigoutsos, I.3    Stephanopoulos, G.4
  • 52
    • 77149155289 scopus 로고    scopus 로고
    • Identification of novel human immunodeficiency virus type 1 inhibitory peptides based on the antimicrobial peptide database
    • Wang, G.; Watson, K.M.; Peterkofsky, A.; Buckheit, R.W., Jr. Identification of novel human immunodeficiency virus type 1 inhibitory peptides based on the antimicrobial peptide database. Antimicrob. Agents Chemother. 2010, 54, 1343-1346.
    • (2010) Antimicrob. Agents Chemother , vol.54 , pp. 1343-1346
    • Wang, G.1    Watson, K.M.2    Peterkofsky, A.3    Buckheit Jr., R.W.4
  • 53
    • 84862819407 scopus 로고    scopus 로고
    • Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300
    • Menousek, J.; Mishra, B.; Hanke, M.L.; Heim, C.E.; Kielian, T.; Wang, G. Database screening and in vivo efficacy of antimicrobial peptides against methicillin-resistant Staphylococcus aureus USA300. Int. J. Antimicrob. Agents 2012, 39, 402-406.
    • (2012) Int. J. Antimicrob. Agents , vol.39 , pp. 402-406
    • Menousek, J.1    Mishra, B.2    Hanke, M.L.3    Heim, C.E.4    Kielian, T.5    Wang, G.6
  • 54
    • 84879811817 scopus 로고    scopus 로고
    • De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop structures
    • doi:10.4172/2155-6113.S2-003
    • Wang, G.; Buckheit, K.W.; Mishra, B.; Lushnikova, T.; Buckheit, R.W., Jr. De Novo Design of Antiviral and Antibacterial Peptides with Varying Loop structures. J. AIDS Clin. Res. 2011, S2:003. doi:10.4172/2155-6113.S2-003.
    • (2011) J. AIDS Clin. Res , vol.S2 , pp. 003
    • Wang, G.1    Buckheit, K.W.2    Mishra, B.3    Lushnikova, T.4    Buckheit Jr., R.W.5
  • 55
    • 84864451396 scopus 로고    scopus 로고
    • Ab initio design of potent anti-MRSA peptides based on database filtering technology
    • Mishra, B.; Wang, G. Ab initio design of potent anti-MRSA peptides based on database filtering technology. J. Am. Chem. Soc. 2012, 134, 12426-12429.
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 12426-12429
    • Mishra, B.1    Wang, G.2
  • 56
    • 50949120543 scopus 로고    scopus 로고
    • Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins
    • Wang, G.; Watson, K.M.; Buckheit, R.W., Jr. Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins. Antimicrob. Agents Chemother. 2008, 52, 3438-3440.
    • (2008) Antimicrob. Agents Chemother , vol.52 , pp. 3438-3440
    • Wang, G.1    Watson, K.M.2    Buckheit Jr., R.W.3
  • 57
    • 84868131857 scopus 로고    scopus 로고
    • Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity
    • Liu, Y.; Xia, X.; Xu, L.; Wang, Y. Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity. Biomaterials 2013, 34, 237-250.
    • (2013) Biomaterials , vol.34 , pp. 237-250
    • Liu, Y.1    Xia, X.2    Xu, L.3    Wang, Y.4
  • 58
    • 84858797510 scopus 로고    scopus 로고
    • Design and characterization of novel hybrid antimicrobial peptides based on cecropin A, LL-37 and magainin II
    • Fox, M.A.; Thwaite, J.E.; Ulaeto, D.O.; Atkins, T.P.; Atkins, H.S. Design and characterization of novel hybrid antimicrobial peptides based on cecropin A, LL-37 and magainin II. Peptides 2012, 33, 197-205.
    • (2012) Peptides , vol.33 , pp. 197-205
    • Fox, M.A.1    Thwaite, J.E.2    Ulaeto, D.O.3    Atkins, T.P.4    Atkins, H.S.5
  • 60
    • 2442470533 scopus 로고    scopus 로고
    • The next generation of HIV/AIDS drugs: Novel and developmental anti-HIV drugs and targets
    • Turpin, J.A. The next generation of HIV/AIDS drugs: Novel and developmental anti-HIV drugs and targets. Expert Rev. Anti Infect. Ther. 2003, 1, 97-128.
    • (2003) Expert Rev. Anti Infect. Ther , vol.1 , pp. 97-128
    • Turpin, J.A.1
  • 61
    • 84876277108 scopus 로고    scopus 로고
    • Factors Important to the Prioritization and Development of Successful Topical Microbicides for HIV-1
    • 2012
    • Buckheit, K.W.; Buckheit, R.W., Jr. Factors Important to the Prioritization and Development of Successful Topical Microbicides for HIV-1. Mol. Biol. Int. 2012, 2012, 781305.
    • (2012) Mol. Biol. Int , pp. 781305
    • Buckheit, K.W.1    Buckheit Jr., R.W.2
  • 62
    • 50549092676 scopus 로고    scopus 로고
    • Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae)
    • Conlon, J.M.; Kolodziejek, J.; Nowotny, N.; Leprince, J.; Vaudry, H.; Coquet, L.; Jouenne, T.; King, J.D. Characterization of antimicrobial peptides from the skin secretions of the Malaysian frogs, Odorrana hosii and Hylarana picturata (Anura:Ranidae). Toxicon 2008, 52, 465-473.
    • (2008) Toxicon , vol.52 , pp. 465-473
    • Conlon, J.M.1    Kolodziejek, J.2    Nowotny, N.3    Leprince, J.4    Vaudry, H.5    Coquet, L.6    Jouenne, T.7    King, J.D.8
  • 63
    • 58149505744 scopus 로고    scopus 로고
    • The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae)
    • Wang, H.; Lu, Y.; Zhang, X.; Hu, Y.; Yu, H.; Liu, J.; Sun, J. The novel antimicrobial peptides from skin of Chinese broad-folded frog, Hylarana latouchii (Anura:Ranidae). Peptides 2009, 30, 273-282.
    • (2009) Peptides , vol.30 , pp. 273-282
    • Wang, H.1    Lu, Y.2    Zhang, X.3    Hu, Y.4    Yu, H.5    Liu, J.6    Sun, J.7
  • 64
    • 27744473974 scopus 로고    scopus 로고
    • Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista
    • Souza, B.M.; Mendes, M.A.; Santos, L.D.; Marques, M.R.; Cesar, L.M.; Almeida, R.N.; Pagnocca, F.C.; Konno, K.; Palma, M.S. Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista. Peptides 2005, 26, 2157-2164.
    • (2005) Peptides , vol.26 , pp. 2157-2164
    • Souza, B.M.1    Mendes, M.A.2    Santos, L.D.3    Marques, M.R.4    Cesar, L.M.5    Almeida, R.N.6    Pagnocca, F.C.7    Konno, K.8    Palma, M.S.9
  • 66
    • 0025001650 scopus 로고
    • All-D-magainin: Chirality, antimicrobial activity and proteolytic resistance
    • Bessalle, R.; Kapitkovsky, A.; Gorea, A.; Shalit, I.; Fridkin, M. All-D-magainin: Chirality, antimicrobial activity and proteolytic resistance. FEBS Lett. 1990, 274, 151-155.
    • (1990) FEBS Lett , vol.274 , pp. 151-155
    • Bessalle, R.1    Kapitkovsky, A.2    Gorea, A.3    Shalit, I.4    Fridkin, M.5
  • 68
    • 0037406076 scopus 로고    scopus 로고
    • Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles
    • Wang, G.; Keifer, P.A.; Peterkofsky, A. Solution structure of the N-terminal amphitropic domain of Escherichia coli glucose-specific enzyme IIA in membrane-mimetic micelles. Protein Sci. 2003, 12, 1087-1096.
    • (2003) Protein Sci , vol.12 , pp. 1087-1096
    • Wang, G.1    Keifer, P.A.2    Peterkofsky, A.3
  • 69
    • 0034704122 scopus 로고    scopus 로고
    • A novel membrane anchor function for the N-terminal amphipathic sequence of the signal-transducing protein IIAGlucose of the Escherichia coli phosphotransferase system
    • Wang, G.; Peterkofsky, A.; Clore, G.M. A novel membrane anchor function for the N-terminal amphipathic sequence of the signal-transducing protein IIAGlucose of the Escherichia coli phosphotransferase system. J. Biol. Chem. 2000, 275, 39811-39814.
    • (2000) J. Biol. Chem , vol.275 , pp. 39811-39814
    • Wang, G.1    Peterkofsky, A.2    Clore, G.M.3
  • 70
    • 0033859322 scopus 로고    scopus 로고
    • The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2
    • Rozek, T.; Wegener, K.L.; Bowie, J.H.; Olver, I.N.; Carver, J.A.; Wallace, J.C.; Tyler, M.J. The antibiotic and anticancer active aurein peptides from the Australian Bell Frogs Litoria aurea and Litoria raniformis the solution structure of aurein 1.2. Eur. J. Biochem. 2000, 267, 5330-5341.
    • (2000) Eur. J. Biochem , vol.267 , pp. 5330-5341
    • Rozek, T.1    Wegener, K.L.2    Bowie, J.H.3    Olver, I.N.4    Carver, J.A.5    Wallace, J.C.6    Tyler, M.J.7
  • 71
    • 57749088664 scopus 로고    scopus 로고
    • Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles
    • Wang, G. Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles. J. Biol. Chem. 2008, 283, 32637-32643.
    • (2008) J. Biol. Chem , vol.283 , pp. 32637-32643
    • Wang, G.1
  • 72
    • 33646597266 scopus 로고    scopus 로고
    • Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region
    • Li, X.; Li, Y.; Han, H.; Miller, D.W.; Wang, G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. J. Am. Chem. Soc. 2006, 128, 5776-5785.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 5776-5785
    • Li, X.1    Li, Y.2    Han, H.3    Miller, D.W.4    Wang, G.5
  • 74
  • 75
    • 57749108450 scopus 로고    scopus 로고
    • NMR studies of a model antimicrobial peptide in the micelles of SDS, dodecylphosphocholine, or dioctanoyl phosphatidylglycerol
    • Wang, G. NMR studies of a model antimicrobial peptide in the micelles of SDS, dodecylphosphocholine, or dioctanoyl phosphatidylglycerol. Open Magn. Reson. J. 2008, 1, 9-15.
    • (2008) Open Magn. Reson. J , vol.1 , pp. 9-15
    • Wang, G.1
  • 77
    • 79955599702 scopus 로고    scopus 로고
    • Biophysical analysis of membrane targeting antimicrobial peptides: Membrane properties and design of peptides specifically targeting Gram-negative bacteria
    • Wang, G., Ed.; CABI: Wallingford, England
    • Epand, R.M.; Epand, R.F. Biophysical analysis of membrane targeting antimicrobial peptides: Membrane properties and design of peptides specifically targeting Gram-negative bacteria. In Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies; Wang, G., Ed.; CABI: Wallingford, England, 2010; pp. 116-127.
    • (2010) Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies , pp. 116-127
    • Epand, R.M.1    Epand, R.F.2
  • 78
    • 67650957816 scopus 로고    scopus 로고
    • New strategies for novel antibiotics: Peptides targeting bacterial cell membranes
    • Lohner, K. New strategies for novel antibiotics: Peptides targeting bacterial cell membranes. Gen. Physiol. Biophys. 2009, 28, 105-116.
    • (2009) Gen. Physiol. Biophys , vol.28 , pp. 105-116
    • Lohner, K.1
  • 82
    • 77951271759 scopus 로고    scopus 로고
    • Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II
    • De Leeuw, E.; Li, C.; Zeng, P.; Li, C.; Diepeveen-de Buin, M.; Lu, W.Y.; Breukink, E.; Lu, W. Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II. FEBS Lett. 2010, 584, 1543-1548.
    • (2010) FEBS Lett , vol.584 , pp. 1543-1548
    • de Leeuw, E.1    Li, C.2    Zeng, P.3    Li, C.4    Diepeveen-De Buin, M.5    Lu, W.Y.6    Breukink, E.7    Lu, W.8
  • 85
    • 84872106766 scopus 로고    scopus 로고
    • Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences
    • Ilić, N.; Novković, M.; Guida, F.; Xhindoli, D.; Benincasa, M.; Tossi, A.; Juretić, D. Selective antimicrobial activity and mode of action of adepantins, glycine-rich peptide antibiotics based on anuran antimicrobial peptide sequences. Biochim. Biophys. Acta 2013, 1828, 1004-1012.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1004-1012
    • Ilić, N.1    Novković, M.2    Guida, F.3    Xhindoli, D.4    Benincasa, M.5    Tossi, A.6    Juretić, D.7
  • 86
    • 84872050769 scopus 로고    scopus 로고
    • Lipid composition is a determinant for human defensin HNP1 selectivity
    • Gonçalves, S.; Abade, J.; Teixeira, A.; Santos, N.C. Lipid composition is a determinant for human defensin HNP1 selectivity. Biopolymers 2012, 98, 313-321.
    • (2012) Biopolymers , vol.98 , pp. 313-321
    • Gonçalves, S.1    Abade, J.2    Teixeira, A.3    Santos, N.C.4
  • 87
    • 0042573730 scopus 로고    scopus 로고
    • New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells
    • Papo, N.; Shai, Y. New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells. Biochemistry 2003, 42, 9346-9354.
    • (2003) Biochemistry , vol.42 , pp. 9346-9354
    • Papo, N.1    Shai, Y.2
  • 88
    • 0031024551 scopus 로고    scopus 로고
    • Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study
    • Oren, Z.; Shai, Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: Structure-function study. Biochemistry 1997, 36, 1826-1835.
    • (1997) Biochemistry , vol.36 , pp. 1826-1835
    • Oren, Z.1    Shai, Y.2
  • 89
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park, C.B.; Kim, H.S.; Kim, S.C. Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 1998, 244, 253-257.
    • (1998) Biochem. Biophys. Res. Commun , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 90
    • 0033037847 scopus 로고    scopus 로고
    • Not only the nature of peptide but also the characteristics of cell membrane determine the antimicrobial mechanism of a peptide
    • Liang, J.F.; Kim, S.C. Not only the nature of peptide but also the characteristics of cell membrane determine the antimicrobial mechanism of a peptide. J. Pept. Res. 1999, 53, 518-522.
    • (1999) J. Pept. Res , vol.53 , pp. 518-522
    • Liang, J.F.1    Kim, S.C.2
  • 91
    • 0017078449 scopus 로고
    • Action of polymyxin B on bacterial membranes: Phosphatidylglycerol- and cardiolipin-induced susceptibility to polymyxin B in Acholeplasma laidlawii B
    • Teuber, M.; Bader, J. Action of polymyxin B on bacterial membranes: Phosphatidylglycerol- and cardiolipin-induced susceptibility to polymyxin B in Acholeplasma laidlawii B. Antimicrob. Agents Chemother. 1976, 9, 26-35.
    • (1976) Antimicrob. Agents Chemother , vol.9 , pp. 26-35
    • Teuber, M.1    Bader, J.2
  • 92
    • 0034713613 scopus 로고    scopus 로고
    • Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: Proline as a translocation promoting factor
    • Kobayashi, S.; Takeshima, K.; Park, C.B.; Kim, S.C.; Matsuzaki, K. Interactions of the novel antimicrobial peptide buforin 2 with lipid bilayers: Proline as a translocation promoting factor. Biochemistry 2000, 39, 8648-8654.
    • (2000) Biochemistry , vol.39 , pp. 8648-8654
    • Kobayashi, S.1    Takeshima, K.2    Park, C.B.3    Kim, S.C.4    Matsuzaki, K.5
  • 93
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • Park, C.B.; Yi, K.S.; Matsuzaki, K.; Kim, M.S.; Kim, S.C. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl. Acad. Sci. USA 2000, 97, 8245-8250.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 94
    • 84855281495 scopus 로고
    • Electron microscopy of the action of polymyxin on leptospirae
    • Bystricky, V.; Ladzianska, K.; Halasa, M. Electron microscopy of the action of polymyxin on leptospirae. J. Bacteriol. 1962, 84, 864-865.
    • (1962) J. Bacteriol , vol.84 , pp. 864-865
    • Bystricky, V.1    Ladzianska, K.2    Halasa, M.3
  • 96
    • 0018621599 scopus 로고
    • Estimation of membrane potentials of individual lymphocytes by flow cytometry
    • Shapiro, H.M.; Natale, P.J.; Kamentsky, L.A. Estimation of membrane potentials of individual lymphocytes by flow cytometry. Proc. Natl. Acad. Sci. USA 1979, 76, 5728-5730.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5728-5730
    • Shapiro, H.M.1    Natale, P.J.2    Kamentsky, L.A.3
  • 97
    • 0033178532 scopus 로고    scopus 로고
    • Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity
    • Oren, Z.; Lerman, J.C.; Gudmundsson, G.H.; Agerberth, B.; Shai, Y. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: Relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 1999, 341(Pt. 3), 501-513.
    • (1999) Biochem. J , vol.341 , Issue.PART 3 , pp. 501-513
    • Oren, Z.1    Lerman, J.C.2    Gudmundsson, G.H.3    Agerberth, B.4    Shai, Y.5
  • 98
    • 0038052326 scopus 로고    scopus 로고
    • Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37
    • Henzler Wildman, K.A.; Lee, D.K.; Ramamoorthy, A. Mechanism of lipid bilayer disruption by the human antimicrobial peptide, LL-37. Biochemistry 2003, 42, 6545-6558.
    • (2003) Biochemistry , vol.42 , pp. 6545-6558
    • Henzler Wildman, K.A.1    Lee, D.K.2    Ramamoorthy, A.3
  • 99
    • 79959644039 scopus 로고    scopus 로고
    • Transmembrane pores formed by human antimicrobial peptide LL-37
    • Lee, C.C.; Sun, Y.; Qian, S.; Huang, H.W. Transmembrane pores formed by human antimicrobial peptide LL-37. Biophys J. 2011, 100, 1688-1696.
    • (2011) Biophys J , vol.100 , pp. 1688-1696
    • Lee, C.C.1    Sun, Y.2    Qian, S.3    Huang, H.W.4
  • 100
    • 84862959893 scopus 로고    scopus 로고
    • Structural studies of antimicrobial peptides provide insight into their mechanisms of action
    • Wang, G. Ed.; CABI: Oxfordshire, England
    • Wang, G. Structural studies of antimicrobial peptides provide insight into their mechanisms of action. In Antimicrobial Peptides: Discovery, Design and Novel Therapeutic strategies; Wang, G. Ed.; CABI: Oxfordshire, England, 2010; 141-168.
    • (2010) Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies , pp. 141-168
    • Wang, G.1
  • 101
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand, R.M.; Vogel, H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1999, 1462, 11-28.
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 102
    • 0036257512 scopus 로고    scopus 로고
    • Molecular diversity in gene-coded, cationic antimicrobial polypeptides
    • Tossi, A.; Sandri, L. Molecular diversity in gene-coded, cationic antimicrobial polypeptides. Curr. Pharm. Des. 2002, 8, 743-761.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 743-761
    • Tossi, A.1    Sandri, L.2
  • 104
    • 0028209429 scopus 로고
    • Structure of micelle-associated alamethicin from 1H-NMR. Evidence for conformational heterogeneity in a voltage-gated peptide
    • Franklin, J.C.; Ellena, J.F.; Jayasinghe, S.; Kelsh, L.P.; Cafiso, D.S. Structure of micelle-associated alamethicin from 1H-NMR. Evidence for conformational heterogeneity in a voltage-gated peptide. Biochemistry 1994, 33, 4036-4045.
    • (1994) Biochemistry , vol.33 , pp. 4036-4045
    • Franklin, J.C.1    Ellena, J.F.2    Jayasinghe, S.3    Kelsh, L.P.4    Cafiso, D.S.5
  • 105
    • 0028335099 scopus 로고
    • Conformation states of gramicidin A along the pathway to the formation of channels in model membranes determined by 2D NMR and circular dichroism spectroscopy
    • Abdul-Manan, N.; Hinton, J.F. Conformation states of gramicidin A along the pathway to the formation of channels in model membranes determined by 2D NMR and circular dichroism spectroscopy. Biochemistry 1994, 33, 6773-6783.
    • (1994) Biochemistry , vol.33 , pp. 6773-6783
    • Abdul-Manan, N.1    Hinton, J.F.2
  • 106
    • 0032997518 scopus 로고    scopus 로고
    • The structure of the antimicrobial active center of lactoferricin B bound to sodium dodecyl sulfate micelles
    • Schibli, D.J.; Hwang, P.M.; Vogel, H.J. The structure of the antimicrobial active center of lactoferricin B bound to sodium dodecyl sulfate micelles. FEBS Lett. 1999, 446, 213-217.
    • (1999) FEBS Lett , vol.446 , pp. 213-217
    • Schibli, D.J.1    Hwang, P.M.2    Vogel, H.J.3
  • 107
    • 84862907676 scopus 로고    scopus 로고
    • Structure, dynamics, antimicrobial and immune modulatory activities of human LL-23 and its single residue variants mutated based on homologous primate cathelicidins
    • Wang, G.; Elliott, M.; Cogen, A.L.; Ezell, E.L.; Gallo, R.L.; Hancock, R.E.W. Structure, dynamics, antimicrobial and immune modulatory activities of human LL-23 and its single residue variants mutated based on homologous primate cathelicidins. Biochemistry 2012, 51, 653-664.
    • (2012) Biochemistry , vol.51 , pp. 653-664
    • Wang, G.1    Elliott, M.2    Cogen, A.L.3    Ezell, E.L.4    Gallo, R.L.5    Hancock, R.E.W.6
  • 108
    • 0028292987 scopus 로고
    • Gramicidin A/short-chain phospholipid dispersions: Chain length dependence of gramicidin conformation and lipid organization
    • Greathouse, D.V.; Hinton, J.F.; Kim, K.S.; Koeppe, R.E., 2nd. Gramicidin A/short-chain phospholipid dispersions: Chain length dependence of gramicidin conformation and lipid organization. Biochemistry 1994, 33, 4291-4299.
    • (1994) Biochemistry , vol.33 , pp. 4291-4299
    • Greathouse, D.V.1    Hinton, J.F.2    Kim, K.S.3    Koeppe II, R.E.4
  • 109
    • 79958087317 scopus 로고    scopus 로고
    • Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K] alyteserin-1c
    • Subasinghage, A.P.; O'Flynn, D.; Conlon, J.M.; Hewage, C.M. Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K] alyteserin-1c. Biochim. Biophys. Acta 2011, 1808, 1975-1984.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1975-1984
    • Subasinghage, A.P.1    O'Flynn, D.2    Conlon, J.M.3    Hewage, C.M.4
  • 110
    • 3042746872 scopus 로고    scopus 로고
    • Effects of detergent alkyl chain length and chemical structure on the properties of a micelle-bound bacterial membrane targeting peptide
    • Keifer, P.A.; Peterkofsky, A.; Wang, G. Effects of detergent alkyl chain length and chemical structure on the properties of a micelle-bound bacterial membrane targeting peptide. Anal. Biochem. 2004, 331, 33-39.
    • (2004) Anal. Biochem , vol.331 , pp. 33-39
    • Keifer, P.A.1    Peterkofsky, A.2    Wang, G.3
  • 111
    • 2442681552 scopus 로고    scopus 로고
    • Short-chain diacyl phosphatidylglycerol: Which one to use for the NMR structural determination of a membrane-associated peptide from Escherichia coli
    • Wang, G.; Keifer, P.A.; Peterkofsky, A. Short-chain diacyl phosphatidylglycerol: Which one to use for the NMR structural determination of a membrane-associated peptide from Escherichia coli? Spectroscopy 2004, 18, 257-264.
    • (2004) Spectroscopy , vol.18 , pp. 257-264
    • Wang, G.1    Keifer, P.A.2    Peterkofsky, A.3
  • 112
    • 36849090536 scopus 로고    scopus 로고
    • Determination of solution structure and lipid micelle location of an engineered membrane peptide by using one NMR experiment and one sample
    • Wang, G. Determination of solution structure and lipid micelle location of an engineered membrane peptide by using one NMR experiment and one sample. Biochim. Biophys. Acta 2007, 1768, 3271-3281.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3271-3281
    • Wang, G.1
  • 113
    • 33646010991 scopus 로고    scopus 로고
    • Structural biology of antimicrobial peptides by NMR
    • Wang, G. Structural biology of antimicrobial peptides by NMR. Curr. Org. Chem. 2006, 10, 569-581.
    • (2006) Curr. Org. Chem , vol.10 , pp. 569-581
    • Wang, G.1
  • 116
    • 77957656356 scopus 로고    scopus 로고
    • High-resolution crystal structure of a lasso peptide
    • Nar, H.; Schmid, A.; Puder, C.; Potterat, O. High-resolution crystal structure of a lasso peptide. ChemMedChem 2010, 5, 1689-1692.
    • (2010) ChemMedChem , vol.5 , pp. 1689-1692
    • Nar, H.1    Schmid, A.2    Puder, C.3    Potterat, O.4
  • 117
    • 84870524827 scopus 로고    scopus 로고
    • Structural characterization of the cyclic cystine ladder motif of θ-defensins
    • Conibear, A.C.; Rosengren, K.J.; Harvery, P.J.; Craik, D.J. Structural characterization of the cyclic cystine ladder motif of θ-defensins. Biochemistry 2012, 51, 9718-9726.
    • (2012) Biochemistry , vol.51 , pp. 9718-9726
    • Conibear, A.C.1    Rosengren, K.J.2    Harvery, P.J.3    Craik, D.J.4
  • 118
    • 0035836463 scopus 로고    scopus 로고
    • Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from Rhesus macaque leukocytes
    • Trabi, M.; Schirra, H.J.; Craik, D.J. Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from Rhesus macaque leukocytes. Biochemistry 2001, 40, 4211-4221.
    • (2001) Biochemistry , vol.40 , pp. 4211-4221
    • Trabi, M.1    Schirra, H.J.2    Craik, D.J.3
  • 119
    • 0028927655 scopus 로고
    • Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1
    • Saether, O.; Craik, D.J.; Campbell, I.D.; Sletten, K.; Juul, J.; Norman, D.G. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1. Biochemistry 1995, 34, 4147-4158.
    • (1995) Biochemistry , vol.34 , pp. 4147-4158
    • Saether, O.1    Craik, D.J.2    Campbell, I.D.3    Sletten, K.4    Juul, J.5    Norman, D.G.6
  • 121
    • 0034727642 scopus 로고    scopus 로고
    • Solution structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1)
    • Yang, Y.S.; Mitta, G.; Chavanieu, A.; Calas, B.; Sanchez, J.F.; Roch, P.; Aumelas, A. Solution structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1). Biochemistry 2000, 39, 14436-14447.
    • (2000) Biochemistry , vol.39 , pp. 14436-14447
    • Yang, Y.S.1    Mitta, G.2    Chavanieu, A.3    Calas, B.4    Sanchez, J.F.5    Roch, P.6    Aumelas, A.7
  • 122
    • 0035188391 scopus 로고    scopus 로고
    • Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity
    • Bauer, F.; Schweimer, K.; Klüver, E.; Conejo-Garcia, J.R.; Forssmann, W.G.; Rösch, P.; Adermann, K.; Sticht, H. Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci. 2001, 10, 2470-2479.
    • (2001) Protein Sci , vol.10 , pp. 2470-2479
    • Bauer, F.1    Schweimer, K.2    Klüver, E.3    Conejo-Garcia, J.R.4    Forssmann, W.G.5    Rösch, P.6    Adermann, K.7    Sticht, H.8
  • 123
    • 0034719121 scopus 로고    scopus 로고
    • Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles
    • Rozek, A.; Friedrich, C.L.; Hancock, R.E. Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles. Biochemistry 2000, 39, 15765-15774.
    • (2000) Biochemistry , vol.39 , pp. 15765-15774
    • Rozek, A.1    Friedrich, C.L.2    Hancock, R.E.3
  • 125
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y.; Delaglio, F.; Cornilescu, G.; Bax, A. TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 2009, 44, 213-223.
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 126
    • 74249106997 scopus 로고    scopus 로고
    • Structure, dynamics and mapping of membrane-binding residues of micelle-bound antimicrobial peptides by natural abundance 13C NMR spectroscopy
    • Wang, G. Structure, dynamics and mapping of membrane-binding residues of micelle-bound antimicrobial peptides by natural abundance 13C NMR spectroscopy. Biochim. Biophys. Acta 2010, 1798, 114-121.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 114-121
    • Wang, G.1
  • 127
    • 34247370223 scopus 로고    scopus 로고
    • A novel method for purifying recombinant human host defense cathelicidin LL-37 by utilizing its inherent property of aggregation
    • Li, Y.; Li, X.; Li, H.; Lockridge, O.; Wang, G. A novel method for purifying recombinant human host defense cathelicidin LL-37 by utilizing its inherent property of aggregation. Protein Expr. Purif. 2007, 54, 157-165.
    • (2007) Protein Expr. Purif , vol.54 , pp. 157-165
    • Li, Y.1    Li, X.2    Li, H.3    Lockridge, O.4    Wang, G.5
  • 128
    • 33646726320 scopus 로고    scopus 로고
    • Cloning, expression, isotope labeling, and purification of human antimicrobial peptide LL-37 in Escherichia coli for NMR studies
    • Li, Y.; Li, X.; Wang, G. Cloning, expression, isotope labeling, and purification of human antimicrobial peptide LL-37 in Escherichia coli for NMR studies. Protein Expr. Purif. 2006, 47, 498-505.
    • (2006) Protein Expr. Purif , vol.47 , pp. 498-505
    • Li, Y.1    Li, X.2    Wang, G.3
  • 129
    • 0025341339 scopus 로고
    • A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin
    • Ikura, M.; Kay, L.E.; Bax, A. A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry 1990, 29, 4659-4667.
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 130
    • 43949083747 scopus 로고    scopus 로고
    • NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles
    • Porcelli, F.; Verardi, R.; Shi, L.; Henzler-Wildman, K.A.; Ramamoorthy, A.; Veglia, G. NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles. Biochemistry 2008, 47, 5565-5572.
    • (2008) Biochemistry , vol.47 , pp. 5565-5572
    • Porcelli, F.1    Verardi, R.2    Shi, L.3    Henzler-Wildman, K.A.4    Ramamoorthy, A.5    Veglia, G.6
  • 132
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptides of human neutrophils
    • Turner, J., Cho, Y., Dinh, N.-N., Waring, A.J., Lehrer, R.I. Activities of LL-37, a cathelin-associated antimicrobial peptides of human neutrophils. Antimicrob. Agents Chemother. 1998, 42, 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
  • 133
    • 79953695041 scopus 로고    scopus 로고
    • Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex
    • Knappe, D.; Zahn, M.; Sauer, U.; Schiffer, G.; Sträter, N.; Hoffmann, R. Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex. ChemBioChem 2011, 12, 874-876.
    • (2011) ChemBioChem , vol.12 , pp. 874-876
    • Knappe, D.1    Zahn, M.2    Sauer, U.3    Schiffer, G.4    Sträter, N.5    Hoffmann, R.6
  • 134
    • 82255172414 scopus 로고    scopus 로고
    • Rediscovering natural products as a source of new drugs
    • Koehn, F.E.; Carter, G.T. Rediscovering natural products as a source of new drugs. Discov. Med. 2005, 5, 159-164.
    • (2005) Discov. Med , vol.5 , pp. 159-164
    • Koehn, F.E.1    Carter, G.T.2
  • 135
    • 0030707561 scopus 로고    scopus 로고
    • Will natural products remain an important source of drug research for the future?
    • Nisbet, L.J.; Moore, M. Will natural products remain an important source of drug research for the future? Curr. Opin. Biotechnol. 1997, 8, 708-712.
    • (1997) Curr. Opin. Biotechnol , vol.8 , pp. 708-712
    • Nisbet, L.J.1    Moore, M.2
  • 136
    • 84878389766 scopus 로고    scopus 로고
    • Database-aided prediction and design of novel antimicrobial peptides
    • Wang, G.; CABI: Wallingford, England
    • Wang, G. Database-aided prediction and design of novel antimicrobial peptides. In Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies; Wang, G.; CABI: Wallingford, England, 2010; pp. 72-86.
    • (2010) Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies , pp. 72-86
    • Wang, G.1
  • 137
    • 0026419319 scopus 로고
    • Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery
    • Houghten, R.A.; Pinilla, C.; Blondelle, S.E.; Appel, J.R.; Dooley, C.T.; Cuervo, J.H. Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery. Nature 1991, 354, 84-86.
    • (1991) Nature , vol.354 , pp. 84-86
    • Houghten, R.A.1    Pinilla, C.2    Blondelle, S.E.3    Appel, J.R.4    Dooley, C.T.5    Cuervo, J.H.6
  • 138
    • 84876556683 scopus 로고    scopus 로고
    • Synthetic Molecular Evolution of Pore-Forming Peptides by Iterative Combinatorial Library Screening
    • Krauson, A.J.; He, J.; Wimley, A.W.; Hoffmann, A.R.; Wimley, W.C. Synthetic Molecular Evolution of Pore-Forming Peptides by Iterative Combinatorial Library Screening. ACS Chem. Biol. 2013, 8, 823-831.
    • (2013) ACS Chem. Biol , vol.8 , pp. 823-831
    • Krauson, A.J.1    He, J.2    Wimley, A.W.3    Hoffmann, A.R.4    Wimley, W.C.5
  • 139
    • 78649813603 scopus 로고    scopus 로고
    • Optimization and high-throughput screening of antimicrobial peptides
    • Blondelle, S.E.; Lohner, K. Optimization and high-throughput screening of antimicrobial peptides. Curr. Pharm. Des. 2010, 16, 3204-3211.
    • (2010) Curr. Pharm. Des , vol.16 , pp. 3204-3211
    • Blondelle, S.E.1    Lohner, K.2
  • 140
    • 35448929949 scopus 로고    scopus 로고
    • Analysis and prediction of antibacterial peptides
    • Lata, S.; Sharma, B.K.; Raghava, G.P. Analysis and prediction of antibacterial peptides. BMC Bioinformatics 2007, 8, 263.
    • (2007) BMC Bioinformatics , vol.8 , pp. 263
    • Lata, S.1    Sharma, B.K.2    Raghava, G.P.3
  • 141
    • 75149184631 scopus 로고    scopus 로고
    • AntiBP2: Improved version of antibacterial peptide prediction
    • Lata, S.; Mishra, N.K.; Raghava, G.P. AntiBP2: Improved version of antibacterial peptide prediction. BMC Bioinformatics 2010, 11, S19.
    • (2010) BMC Bioinformatics , vol.11
    • Lata, S.1    Mishra, N.K.2    Raghava, G.P.3
  • 142
    • 84877142829 scopus 로고    scopus 로고
    • Prediction of antimicrobial activity of synthetic peptides by a decision tree model
    • Lira, F.; Perez, P.S.; Baranauskas, J.A.; Nozawa, S.R. Prediction of antimicrobial activity of synthetic peptides by a decision tree model. Appl. Environ. Microbiol. 2013, 79, 3156-3159.
    • (2013) Appl. Environ. Microbiol , vol.79 , pp. 3156-3159
    • Lira, F.1    Perez, P.S.2    Baranauskas, J.A.3    Nozawa, S.R.4
  • 143
    • 84875074764 scopus 로고    scopus 로고
    • IAMP-2L: A two-level multi-label classifier for identifying antimicrobial peptides and their functional types
    • Xiao, X.; Wang, P.; Lin, W.Z.; Jia, J.H.; Chou, K.C. iAMP-2L: A two-level multi-label classifier for identifying antimicrobial peptides and their functional types. Anal. Biochem. 2013, 436, 168-177.
    • (2013) Anal. Biochem , vol.436 , pp. 168-177
    • Xiao, X.1    Wang, P.2    Lin, W.Z.3    Jia, J.H.4    Chou, K.C.5
  • 144
    • 84878221453 scopus 로고    scopus 로고
    • Stepwise identification of potent antimicrobial peptides from human genome
    • doi:10.1016/j.biosystems.2013.03.021
    • Yan, L.; Yan, Y.; Liu, H.; Lv, Q. Stepwise identification of potent antimicrobial peptides from human genome. Biosystems 2013, doi:10.1016/j.biosystems.2013.03.021.
    • (2013) Biosystems
    • Yan, L.1    Yan, Y.2    Liu, H.3    Lv, Q.4
  • 145
    • 34249858459 scopus 로고    scopus 로고
    • AMPer: A database and an automated discovery tool for antimicrobial peptides
    • Fjell, C.D.; Hancock, R.E.; Cherkasov, A. AMPer: A database and an automated discovery tool for antimicrobial peptides. Bioinformatics 2007, 23, 1148-1155.
    • (2007) Bioinformatics , vol.23 , pp. 1148-1155
    • Fjell, C.D.1    Hancock, R.E.2    Cherkasov, A.3
  • 146
    • 0030046733 scopus 로고    scopus 로고
    • Comparison of lantibiotic gene clusters and encoded proteins
    • Siezen, R.J.; Kuipers, O.P.; de Vos, W.M. Comparison of lantibiotic gene clusters and encoded proteins. Antonie Van Leeuwenhoek 1996, 69, 171-184.
    • (1996) Antonie Van Leeuwenhoek , vol.69 , pp. 171-184
    • Siezen, R.J.1    Kuipers, O.P.2    de Vos, W.M.3
  • 149
    • 84872433200 scopus 로고    scopus 로고
    • Effect of antimicrobial peptides derived from human cathelicidin LL-37 on Entamoeba histolytica trophozoites
    • Rico-Mata, R.; de Leon-Rodriguez, L.M.; Avila, E.E. Effect of antimicrobial peptides derived from human cathelicidin LL-37 on Entamoeba histolytica trophozoites. Exp. Parasitol. 2013, 133, 300-306.
    • (2013) Exp. Parasitol , vol.133 , pp. 300-306
    • Rico-Mata, R.1    de Leon-Rodriguez, L.M.2    Avila, E.E.3
  • 150
    • 84874040996 scopus 로고    scopus 로고
    • α-Helix Mimicry with α/β-Peptides
    • Johnson, L.M.; Gellman, S.H. α-Helix Mimicry with α/β-Peptides. Methods Enzymol. 2013, 523, 407-429.
    • (2013) Methods Enzymol , vol.523 , pp. 407-429
    • Johnson, L.M.1    Gellman, S.H.2
  • 152
    • 79960934532 scopus 로고    scopus 로고
    • Short native antimicrobial peptides and engineered ultrashort lipopeptides: Similarities and differences in cell specificities and modes of action
    • Mangoni, M.L.; Shai, Y. Short native antimicrobial peptides and engineered ultrashort lipopeptides: Similarities and differences in cell specificities and modes of action. Cell. Mol. Life Sci. 2011, 68, 2267-2280.
    • (2011) Cell. Mol. Life Sci , vol.68 , pp. 2267-2280
    • Mangoni, M.L.1    Shai, Y.2
  • 153
    • 84878402118 scopus 로고    scopus 로고
    • Chemical modifications of natural antimicrobial peptides and strategies for peptide engineering
    • Wang, G. Chemical modifications of natural antimicrobial peptides and strategies for peptide engineering. Curr. Biotechnol. 2012, 1, 72-79.
    • (2012) Curr. Biotechnol , vol.1 , pp. 72-79
    • Wang, G.1
  • 155
    • 84871019068 scopus 로고    scopus 로고
    • Design of a novel cyclotide-based CXCR4 antagonist with anti-human immunodeficiency virus (HIV)-1 activity
    • Aboye, T.L.; Ha, H.; Majumder, S.; Christ, F.; Debyser, Z.; Shekhtman, A.; Neamati, N.; Camarero, J.A. Design of a novel cyclotide-based CXCR4 antagonist with anti-human immunodeficiency virus (HIV)-1 activity. J. Med. Chem. 2012, 55, 10729-10734.
    • (2012) J. Med. Chem , vol.55 , pp. 10729-10734
    • Aboye, T.L.1    Ha, H.2    Majumder, S.3    Christ, F.4    Debyser, Z.5    Shekhtman, A.6    Neamati, N.7    Camarero, J.A.8
  • 156
    • 84861615565 scopus 로고    scopus 로고
    • Orally active peptidic bradykinin B1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment
    • Wong, C.T.; Rowlands, D.K.; Wong, C.H.; Lo, T.W.; Nguyen, G.K.; Li, H.Y.; Tam, J.P. Orally active peptidic bradykinin B1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment. Angew. Chem. Int. Ed. Engl. 2012, 51, 5620-5624.
    • (2012) Angew. Chem. Int. Ed. Engl , vol.51 , pp. 5620-5624
    • Wong, C.T.1    Rowlands, D.K.2    Wong, C.H.3    Lo, T.W.4    Nguyen, G.K.5    Li, H.Y.6    Tam, J.P.7
  • 158
    • 0033790259 scopus 로고    scopus 로고
    • Development of daptomycin for gram-positive infections
    • Tally, F.P.; DeBruin, M.F. Development of daptomycin for gram-positive infections. J. Antimicrob. Chemother. 2000, 46, 523-526.
    • (2000) J. Antimicrob. Chemother , vol.46 , pp. 523-526
    • Tally, F.P.1    Debruin, M.F.2
  • 160
    • 84857770864 scopus 로고    scopus 로고
    • Daptomycin: A review of properties, clinical use, drug delivery and resistance
    • Vilhena, C.; Bettencourt, A. Daptomycin: A review of properties, clinical use, drug delivery and resistance. Mini Rev. Med. Chem. 2012, 12, 202-209.
    • (2012) Mini Rev. Med. Chem , vol.12 , pp. 202-209
    • Vilhena, C.1    Bettencourt, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.