메뉴 건너뛰기




Volumn 47, Issue 11, 2015, Pages 2385-2397

Antimicrobial activity and membrane-active mechanism of tryptophan zipper-like β-hairpin antimicrobial peptides

Author keywords

Antimicrobial peptides; Bactericidal mechanism; Cell selectivity; Tryptophan zipper; Hairpin

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT; TRYPTOPHAN ZIPPER LIKE BETA HAIRPIN ANTIMICROBIAL PEPTIDE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; TRYPTOPHAN;

EID: 84945465583     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-015-2029-7     Document Type: Article
Times cited : (56)

References (46)
  • 1
    • 77649273799 scopus 로고    scopus 로고
    • Isolation and molecular cloning of venom peptides from Orancistrocerus drewseni (Hymenoptera: Eumenidae)
    • 1:CAS:528:DC%2BC3cXhvFamt7w%3D 19857508
    • Baek JH, Lee SH (2010) Isolation and molecular cloning of venom peptides from Orancistrocerus drewseni (Hymenoptera: Eumenidae). Toxicon 55:711-718
    • (2010) Toxicon , vol.55 , pp. 711-718
    • Baek, J.H.1    Lee, S.H.2
  • 2
    • 0038141960 scopus 로고    scopus 로고
    • Arming the enemy: The evolution of resistance to self-proteins
    • 1:CAS:528:DC%2BD3sXkvFSjtrc%3D 12777478
    • Bell G, Gouyon PH (2003) Arming the enemy: the evolution of resistance to self-proteins. Microbiology 149:1367-1375
    • (2003) Microbiology , vol.149 , pp. 1367-1375
    • Bell, G.1    Gouyon, P.H.2
  • 3
    • 80051546187 scopus 로고    scopus 로고
    • Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?
    • 3159164 1:CAS:528:DC%2BC3MXpvFSmur8%3D 21733662
    • Brogden NK, Brogden KA (2011) Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals? Int J Antimicrob Agents 38:217-225
    • (2011) Int J Antimicrob Agents , vol.38 , pp. 217-225
    • Brogden, N.K.1    Brogden, K.A.2
  • 4
    • 0041624420 scopus 로고    scopus 로고
    • A designed β-hairpin peptide for molecular recognition of ATP in water
    • 1:CAS:528:DC%2BD3sXlsFOhsbo%3D 12904011
    • Butterfield SM, Waters ML (2003) A designed β-hairpin peptide for molecular recognition of ATP in water. J Am Chem Soc 125:9580-9581
    • (2003) J Am Chem Soc , vol.125 , pp. 9580-9581
    • Butterfield, S.M.1    Waters, M.L.2
  • 5
    • 34247153326 scopus 로고    scopus 로고
    • Role of peptide hydrophobicity in the mechanism of action of α-helical antimicrobial peptides
    • 1855469 1:CAS:528:DC%2BD2sXktlOjtLY%3D 17158938
    • Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS (2007) Role of peptide hydrophobicity in the mechanism of action of α-helical antimicrobial peptides. Antimicrob Agents Chemother 51:1398-1406
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 1398-1406
    • Chen, Y.1    Guarnieri, M.T.2    Vasil, A.I.3    Vasil, M.L.4    Mant, C.T.5    Hodges, R.S.6
  • 6
    • 84890159779 scopus 로고    scopus 로고
    • Molecular mechanisms of anticancer action and cell selectivity of short α-helical peptides
    • 1:CAS:528:DC%2BC3sXhslyrtrnL 24246647
    • Chen C, Hu J, Zeng P, Pan F, Yaseen M, Xu H, Lu JR (2014) Molecular mechanisms of anticancer action and cell selectivity of short α-helical peptides. Biomaterials 35:1552-1561
    • (2014) Biomaterials , vol.35 , pp. 1552-1561
    • Chen, C.1    Hu, J.2    Zeng, P.3    Pan, F.4    Yaseen, M.5    Xu, H.6    Lu, J.R.7
  • 7
    • 46049119398 scopus 로고    scopus 로고
    • Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp
    • 1:CAS:528:DC%2BD1cXotlCnsbw%3D 18586467
    • Chou HT et al (2008) Design and synthesis of cationic antimicrobial peptides with improved activity and selectivity against Vibrio spp. Int J Antimicrob Agents 32:130-138
    • (2008) Int J Antimicrob Agents , vol.32 , pp. 130-138
    • Chou, H.T.1
  • 8
    • 0035826776 scopus 로고    scopus 로고
    • Tryptophan zippers: Stable, monomeric β-hairpins
    • 33255 1:CAS:528:DC%2BD3MXjs1Wnsrs%3D 11331745
    • Cochran AG, Skelton NJ, Starovasnik MA (2001) Tryptophan zippers: stable, monomeric β-hairpins. Proc Natl Acad Sci 98:5578-5583
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 5578-5583
    • Cochran, A.G.1    Skelton, N.J.2    Starovasnik, M.A.3
  • 10
    • 84861123585 scopus 로고    scopus 로고
    • Strand length-dependent antimicrobial activity and membrane-active mechanism of arginine-and valine-rich β-hairpin-like antimicrobial peptides
    • 3370809 1:CAS:528:DC%2BC38XnslWrtr0%3D 22391533
    • Dong N, Ma Q, Shan A, Lv Y, Hu W, Gu Y, Li Y (2012) Strand length-dependent antimicrobial activity and membrane-active mechanism of arginine-and valine-rich β-hairpin-like antimicrobial peptides. Antimicrob Agents Chemother 56:2994-3003
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 2994-3003
    • Dong, N.1    Ma, Q.2    Shan, A.3    Lv, Y.4    Hu, W.5    Gu, Y.6    Li, Y.7
  • 11
    • 84903454580 scopus 로고    scopus 로고
    • Antimicrobial potency and selectivity of simplified symmetric-end peptides
    • 1:CAS:528:DC%2BC2cXhtVWqs7nM 24952979
    • Dong N, Zhu X, Chou S, Shan A, Li W, Jiang J (2014) Antimicrobial potency and selectivity of simplified symmetric-end peptides. Biomaterials 35:8028-8039
    • (2014) Biomaterials , vol.35 , pp. 8028-8039
    • Dong, N.1    Zhu, X.2    Chou, S.3    Shan, A.4    Li, W.5    Jiang, J.6
  • 12
    • 66149086931 scopus 로고    scopus 로고
    • Very short peptides with stable folds: Building on the interrelationship of Trp/Trp, Trp/cation, and Trp/backbone-amide interaction geometries
    • 1:CAS:528:DC%2BD1MXjsVahsr0%3D
    • Eidenschink L, Kier BL, Huggins KNL, Andersen NH (2009) Very short peptides with stable folds: building on the interrelationship of Trp/Trp, Trp/cation, and Trp/backbone-amide interaction geometries. Proteins Struct Funct Bioinform 75:308-322
    • (2009) Proteins Struct Funct Bioinform , vol.75 , pp. 308-322
    • Eidenschink, L.1    Kier, B.L.2    Huggins, K.N.L.3    Andersen, N.H.4
  • 14
    • 84877287392 scopus 로고    scopus 로고
    • Effect of repetitive lysine-tryptophan motifs on the bactericidal activity of antimicrobial peptides
    • 3549253 1:CAS:528:DC%2BC3sXhtFyiurk%3D 22914980
    • Gopal R, Seo CH, Song PI, Park Y (2013) Effect of repetitive lysine-tryptophan motifs on the bactericidal activity of antimicrobial peptides. Amino Acids 44:645-660
    • (2013) Amino Acids , vol.44 , pp. 645-660
    • Gopal, R.1    Seo, C.H.2    Song, P.I.3    Park, Y.4
  • 15
    • 0038546798 scopus 로고    scopus 로고
    • Optical spectroscopic investigations of model β-sheet hairpins in aqueous solution
    • 1:CAS:528:DC%2BD3sXktFGqt7o%3D 12812496
    • Hilario J, Kubelka J, Keiderling TA (2003) Optical spectroscopic investigations of model β-sheet hairpins in aqueous solution. J Am Chem Soc 125:7562-7574
    • (2003) J Am Chem Soc , vol.125 , pp. 7562-7574
    • Hilario, J.1    Kubelka, J.2    Keiderling, T.A.3
  • 16
    • 84884252121 scopus 로고    scopus 로고
    • Designed trpzip-3 β-hairpin inhibits amyloid formation in two different amyloid systems
    • 4027462 1:CAS:528:DC%2BC3sXht1SlsbzL 24900756
    • Hopping G, Kellock J, Caughey B, Daggett V (2013) Designed trpzip-3 β-hairpin inhibits amyloid formation in two different amyloid systems. ACS Med Chem Lett 4:824-828
    • (2013) ACS Med Chem Lett , vol.4 , pp. 824-828
    • Hopping, G.1    Kellock, J.2    Caughey, B.3    Daggett, V.4
  • 17
    • 79952614254 scopus 로고    scopus 로고
    • Rational design of α-helical antimicrobial peptides to target gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: Utilization of charge, 'specificity determinants', total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio
    • 3063396 21219588
    • Jiang Z, Vasil AI, Gera L, Vasil ML, Hodges RS (2011) Rational design of α-helical antimicrobial peptides to target gram-negative pathogens, Acinetobacter baumannii and Pseudomonas aeruginosa: utilization of charge, 'specificity determinants', total hydrophobicity, hydrophobe type and location as design parameters to improve the therapeutic ratio. Chem Biol Drug Des 77:225-240
    • (2011) Chem Biol Drug des , vol.77 , pp. 225-240
    • Jiang, Z.1    Vasil, A.I.2    Gera, L.3    Vasil, M.L.4    Hodges, R.S.5
  • 18
    • 28844467956 scopus 로고    scopus 로고
    • Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic β-sheet and α-helical potentials
    • 1315945 1:CAS:528:DC%2BD2MXhtlSqsr%2FI 16304158
    • Jin Y, Hammer J, Pate M, Zhang Y, Zhu F, Zmuda E, Blazyk J (2005) Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic β-sheet and α-helical potentials. Antimicrob Agents Chemother 49:4957-4964
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4957-4964
    • Jin, Y.1    Hammer, J.2    Pate, M.3    Zhang, Y.4    Zhu, F.5    Zmuda, E.6    Blazyk, J.7
  • 19
    • 84863136169 scopus 로고    scopus 로고
    • Bio-inspired design and potential biomedical applications of a novel class of high-affinity peptides
    • 1:CAS:528:DC%2BC38XhtFahtLw%3D
    • Kim S, Kim D, Jung HH, Lee IH, Kim JIL, Suh JY, Jon S (2012) Bio-inspired design and potential biomedical applications of a novel class of high-affinity peptides. Angew Chem Int Ed 51:1890-1894
    • (2012) Angew Chem Int Ed , vol.51 , pp. 1890-1894
    • Kim, S.1    Kim, D.2    Jung, H.H.3    Lee, I.H.4    Kim, J.I.L.5    Suh, J.Y.6    Jon, S.7
  • 21
    • 84868131857 scopus 로고    scopus 로고
    • Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity
    • 1:CAS:528:DC%2BC38XhsVKksL7J 23046754
    • Liu Y, Xia X, Xu L, Wang Y (2013) Design of hybrid β-hairpin peptides with enhanced cell specificity and potent anti-inflammatory activity. Biomaterials 34:237-250
    • (2013) Biomaterials , vol.34 , pp. 237-250
    • Liu, Y.1    Xia, X.2    Xu, L.3    Wang, Y.4
  • 22
    • 84868200797 scopus 로고    scopus 로고
    • Prediction of protein secondary structure from circular dichroism using theoretically derived spectra
    • 1:CAS:528:DC%2BC3MXhsVOisLbP
    • Louis-Jeune C, Andrade-Navarro MA, Perez-Iratxeta C (2012) Prediction of protein secondary structure from circular dichroism using theoretically derived spectra. Proteins Struct Funct Bioinform 80:374-381
    • (2012) Proteins Struct Funct Bioinform , vol.80 , pp. 374-381
    • Louis-Jeune, C.1    Andrade-Navarro, M.A.2    Perez-Iratxeta, C.3
  • 23
    • 84903374874 scopus 로고    scopus 로고
    • Antimicrobial properties and membrane-active mechanism of a potential α-helical antimicrobial derived from cathelicidin PMAP-36
    • 3897731 24466055
    • Lv Y, Wang J, Gao H, Wang Z, Dong N, Ma Q, Shan A (2014) Antimicrobial properties and membrane-active mechanism of a potential α-helical antimicrobial derived from cathelicidin PMAP-36. PLoS One 9:e86364
    • (2014) PLoS One , vol.9 , pp. e86364
    • Lv, Y.1    Wang, J.2    Gao, H.3    Wang, Z.4    Dong, N.5    Ma, Q.6    Shan, A.7
  • 24
    • 84872714452 scopus 로고    scopus 로고
    • Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units
    • 1:CAS:528:DC%2BC38Xhs1Ght73E 22699557
    • Ma QQ et al (2012) Biochemical property and membrane-peptide interactions of de novo antimicrobial peptides designed by helix-forming units. Amino Acids 43:2527-2536
    • (2012) Amino Acids , vol.43 , pp. 2527-2536
    • Ma, Q.Q.1
  • 25
    • 84876668699 scopus 로고    scopus 로고
    • Rational design of cationic antimicrobial peptides by the tandem of leucine-rich repeat
    • 1:CAS:528:DC%2BC3sXktVOhs7k%3D 23430306
    • Ma QQ, Lv YF, Gu Y, Dong N, Li DS, Shan AS (2013) Rational design of cationic antimicrobial peptides by the tandem of leucine-rich repeat. Amino Acids 44:1215-1224
    • (2013) Amino Acids , vol.44 , pp. 1215-1224
    • Ma, Q.Q.1    Lv, Y.F.2    Gu, Y.3    Dong, N.4    Li, D.S.5    Shan, A.S.6
  • 26
    • 65549132784 scopus 로고    scopus 로고
    • Disulfide Bonds versus Trp... Trp pairs in irregular β-hairpins: NMR structure of vammin loop 3-derived peptides as a case study
    • 1:CAS:528:DC%2BD1MXktVajtb8%3D 19294654
    • Mirassou Y, Santiveri CM, Pérez de Vega MJ, González-Muñiz R, Jiménez M (2009) Disulfide Bonds versus Trp... Trp pairs in irregular β-hairpins: NMR structure of vammin loop 3-derived peptides as a case study. Chembiochem 10:902-910
    • (2009) Chembiochem , vol.10 , pp. 902-910
    • Mirassou, Y.1    Santiveri, C.M.2    Pérez De Vega, M.J.3    González-Muñiz, R.4    Jiménez, M.5
  • 27
    • 17744387944 scopus 로고    scopus 로고
    • De novo design of a redox-active minimal rubredoxin mimic
    • 1:CAS:528:DC%2BD2MXivV2ntrY%3D 15839675
    • Nanda V et al (2005) De novo design of a redox-active minimal rubredoxin mimic. J Am Chem Soc 127:5804-5805
    • (2005) J Am Chem Soc , vol.127 , pp. 5804-5805
    • Nanda, V.1
  • 28
    • 77958581350 scopus 로고    scopus 로고
    • Serum stabilities of short tryptophan-and arginine-rich antimicrobial peptide analogs
    • 2937036 20844765
    • Nguyen LT, Chau JK, Perry NA, De Boer L, Zaat SAJ, Vogel HJ (2010) Serum stabilities of short tryptophan-and arginine-rich antimicrobial peptide analogs. PLoS One 5:e12684
    • (2010) PLoS One , vol.5 , pp. e12684
    • Nguyen, L.T.1    Chau, J.K.2    Perry, N.A.3    De Boer, L.4    Zaat, S.A.J.5    Vogel, H.J.6
  • 29
    • 16844380609 scopus 로고    scopus 로고
    • Effect of chain length of cationic model peptides on antibacterial activity
    • 1:CAS:528:DC%2BD2MXivVGjs7c%3D
    • Niidome T, Matsuyama N, Kunihara M, Hatakeyama T, Aoyagi H (2005) Effect of chain length of cationic model peptides on antibacterial activity. Bull Chem Soc Japan 78:473-476
    • (2005) Bull Chem Soc Japan , vol.78 , pp. 473-476
    • Niidome, T.1    Matsuyama, N.2    Kunihara, M.3    Hatakeyama, T.4    Aoyagi, H.5
  • 30
  • 31
    • 84881120375 scopus 로고    scopus 로고
    • Short synthetic β-sheet forming peptide amphiphiles as broad spectrum antimicrobials with antibiofilm and endotoxin neutralizing capabilities
    • 1:CAS:528:DC%2BC3sXjtVegu7Y%3D
    • Ong ZY, Gao SJ, Yang YY (2013) Short synthetic β-sheet forming peptide amphiphiles as broad spectrum antimicrobials with antibiofilm and endotoxin neutralizing capabilities. Adv Funct Mater 23:3682-3692
    • (2013) Adv Funct Mater , vol.23 , pp. 3682-3692
    • Ong, Z.Y.1    Gao, S.J.2    Yang, Y.Y.3
  • 32
    • 84888439590 scopus 로고    scopus 로고
    • Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles
    • 1:CAS:528:DC%2BC3sXhslCmsL3P 24211081
    • Ong ZY, Cheng J, Huang Y, Xu K, Ji Z, Fan W, Yang YY (2014) Effect of stereochemistry, chain length and sequence pattern on antimicrobial properties of short synthetic β-sheet forming peptide amphiphiles. Biomaterials 35:1315-1325
    • (2014) Biomaterials , vol.35 , pp. 1315-1325
    • Ong, Z.Y.1    Cheng, J.2    Huang, Y.3    Xu, K.4    Ji, Z.5    Fan, W.6    Yang, Y.Y.7
  • 33
    • 61749102822 scopus 로고    scopus 로고
    • Design of highly stabilized β-hairpin peptides through cation-π interactions of lysine and N-methyllysine with an aromatic pocket
    • 2649769 1:CAS:528:DC%2BD1MXhtlehtbg%3D 19191524
    • Riemen AJ, Waters ML (2009) Design of highly stabilized β-hairpin peptides through cation-π interactions of lysine and N-methyllysine with an aromatic pocket. Biochemistry 48:1525-1531
    • (2009) Biochemistry , vol.48 , pp. 1525-1531
    • Riemen, A.J.1    Waters, M.L.2
  • 34
    • 79952645597 scopus 로고    scopus 로고
    • Tryptophan residues: Scarce in proteins but strong stabilizers of β-hairpin peptides
    • 1:CAS:528:DC%2BC3cXhsFOmsrrN
    • Santiveri CM, Jiménez M (2010) Tryptophan residues: scarce in proteins but strong stabilizers of β-hairpin peptides. Pept Sci 94:779-790
    • (2010) Pept Sci , vol.94 , pp. 779-790
    • Santiveri, C.M.1    Jiménez, M.2
  • 35
    • 38149106504 scopus 로고    scopus 로고
    • Context-dependence of the contribution of disulfide bonds to β-hairpin stability
    • 1:CAS:528:DC%2BD1cXkvF2ntbw%3D
    • Santiveri CM, Leon E, Rico M, Jiménez M (2008) Context-dependence of the contribution of disulfide bonds to β-hairpin stability. Chemistry A Eur J 14:488-499
    • (2008) Chemistry A Eur J , vol.14 , pp. 488-499
    • Santiveri, C.M.1    Leon, E.2    Rico, M.3    Jiménez, M.4
  • 36
    • 79960361006 scopus 로고    scopus 로고
    • Trp-Trp pairs as β-hairpin stabilisers: Hydrogen-bonded versus non-hydrogen-bonded sites
    • 1:CAS:528:DC%2BC3MXoslOkur0%3D 21670842
    • Santiveri CM, de Vega MJP, González-Muñiz R, Jiménez MA (2011) Trp-Trp pairs as β-hairpin stabilisers: hydrogen-bonded versus non-hydrogen-bonded sites. Org Biomol Chem 9:5487-5492
    • (2011) Org Biomol Chem , vol.9 , pp. 5487-5492
    • Santiveri, C.M.1    De Vega, M.J.P.2    González-Muñiz, R.3    Jiménez, M.A.4
  • 37
    • 77955846576 scopus 로고    scopus 로고
    • Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity
    • 1:CAS:528:DC%2BC3cXhtVKgs7fE 20188791
    • Takahashi D, Shukla SK, Prakash O, Zhang G (2010) Structural determinants of host defense peptides for antimicrobial activity and target cell selectivity. Biochimie 92:1236-1241
    • (2010) Biochimie , vol.92 , pp. 1236-1241
    • Takahashi, D.1    Shukla, S.K.2    Prakash, O.3    Zhang, G.4
  • 38
    • 61749093139 scopus 로고    scopus 로고
    • Relationship between hydrophobic interactions and secondary structure stability for trpzip β-hairpin peptides
    • 1:CAS:528:DC%2BD1MXhtVOgsbs%3D 19173596
    • Takekiyo T, Wu L, Yoshimura Y, Shimizu A, Keiderling TA (2009) Relationship between hydrophobic interactions and secondary structure stability for trpzip β-hairpin peptides. Biochemistry 48:1543-1552
    • (2009) Biochemistry , vol.48 , pp. 1543-1552
    • Takekiyo, T.1    Wu, L.2    Yoshimura, Y.3    Shimizu, A.4    Keiderling, T.A.5
  • 39
    • 84925296673 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptide LL-37 augments IFN-β expression and anti-viral activity induced by double-stranded RNA in keratinocytes
    • 1:CAS:528:DC%2BC2cXhsF2nurzI 24601852
    • Takiguchi T, Morizane S, Yamamoto T, Kajita A, Ikeda K, Iwatsuki K (2014) Cathelicidin antimicrobial peptide LL-37 augments IFN-β expression and anti-viral activity induced by double-stranded RNA in keratinocytes. Br J Dermatol 171:492-498
    • (2014) Br J Dermatol , vol.171 , pp. 492-498
    • Takiguchi, T.1    Morizane, S.2    Yamamoto, T.3    Kajita, A.4    Ikeda, K.5    Iwatsuki, K.6
  • 40
    • 84856774559 scopus 로고    scopus 로고
    • Role of lipids in the interaction of antimicrobial peptides with membranes
    • 1:CAS:528:DC%2BC38XisFCktrw%3D 22245454
    • Teixeira V, Feio MJ, Bastos M (2012) Role of lipids in the interaction of antimicrobial peptides with membranes. Prog Lipid Res 51:149-177
    • (2012) Prog Lipid Res , vol.51 , pp. 149-177
    • Teixeira, V.1    Feio, M.J.2    Bastos, M.3
  • 41
    • 84864562079 scopus 로고    scopus 로고
    • Antimicrobial peptide action on parasites
    • 1:CAS:528:DC%2BC38Xht1Wjs7rP 22664071
    • Torrent M, Pulido D, Rivas L, Andreu D (2012) Antimicrobial peptide action on parasites. Curr Drug Targets 13:1138-1147
    • (2012) Curr Drug Targets , vol.13 , pp. 1138-1147
    • Torrent, M.1    Pulido, D.2    Rivas, L.3    Andreu, D.4
  • 42
    • 78651445030 scopus 로고    scopus 로고
    • Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents
    • 1:CAS:528:DC%2BC3MXmtVOmsQ%3D%3D 21168911
    • Wiradharma N, Khoe U, Hauser CAE, Seow SV, Zhang S, Yang YY (2011) Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents. Biomaterials 32:2204-2212
    • (2011) Biomaterials , vol.32 , pp. 2204-2212
    • Wiradharma, N.1    Khoe, U.2    Hauser, C.A.E.3    Seow, S.V.4    Zhang, S.5    Yang, Y.Y.6
  • 43
    • 70350495817 scopus 로고    scopus 로고
    • Role of tryptophan-tryptophan interactions in trpzip β-hairpin formation, structure, and stability
    • 1:CAS:528:DC%2BD1MXht1GgsbzL 19788311
    • Wu L, McElheny D, Huang R, Keiderling TA (2009) Role of tryptophan-tryptophan interactions in trpzip β-hairpin formation, structure, and stability. Biochemistry 48:10362-10371
    • (2009) Biochemistry , vol.48 , pp. 10362-10371
    • Wu, L.1    McElheny, D.2    Huang, R.3    Keiderling, T.A.4
  • 44
    • 83555176386 scopus 로고    scopus 로고
    • Role of different β-turns in β-hairpin conformation and stability studied by optical spectroscopy
    • 1:CAS:528:DC%2BC3MXhs1SgurzN
    • Wu L, McElheny D, Setnicka V, Hilario J, Keiderling TA (2012) Role of different β-turns in β-hairpin conformation and stability studied by optical spectroscopy. Proteins Struct Funct Bioinform 80:44-60
    • (2012) Proteins Struct Funct Bioinform , vol.80 , pp. 44-60
    • Wu, L.1    McElheny, D.2    Setnicka, V.3    Hilario, J.4    Keiderling, T.A.5
  • 45
    • 33748933561 scopus 로고    scopus 로고
    • Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationship studies
    • 1:CAS:528:DC%2BD28XhtVanu7bF 16678118
    • Zelezetsky I, Tossi A (2006) Alpha-helical antimicrobial peptides-using a sequence template to guide structure-activity relationship studies. Biochim Biophys Acta 1758:1436-1449
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1436-1449
    • Zelezetsky, I.1    Tossi, A.2
  • 46
    • 84888645761 scopus 로고    scopus 로고
    • Design of imperfectly amphipathic α-helical antimicrobial peptides with enhanced cell selectivity
    • 1:CAS:528:DC%2BC3sXhsFCitrrM 24021230
    • Zhu X, Dong N, Wang Z, Ma Z, Zhang L, Ma Q, Shan A (2014) Design of imperfectly amphipathic α-helical antimicrobial peptides with enhanced cell selectivity. Acta Biomater 10:244-257
    • (2014) Acta Biomater , vol.10 , pp. 244-257
    • Zhu, X.1    Dong, N.2    Wang, Z.3    Ma, Z.4    Zhang, L.5    Ma, Q.6    Shan, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.