메뉴 건너뛰기




Volumn 56, Issue 9, 2013, Pages 1307-1314

Comparison on effect of hydrophobicity on the antibacterial and antifungal activities of α-helical antimicrobial peptides

Author keywords

antimicrobial peptide; hydrophobicity; mode of action; net charge; specificity

Indexed keywords

ANTI-BACTERIAL ACTIVITY; ANTI-MICROBIAL ACTIVITY; ANTIBACTERIAL AND ANTIFUNGAL ACTIVITY; ANTIMICROBIAL PEPTIDE; GRAM-POSITIVE BACTERIUM; MODE OF ACTION; NET CHARGES; SPECIFICITY;

EID: 84883456752     PISSN: 16747291     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11426-013-4884-y     Document Type: Article
Times cited : (31)

References (23)
  • 1
    • 84865431287 scopus 로고    scopus 로고
    • Overview on the recent study of antimicrobial peptides: Origins, functions, relative mechanisms and application
    • 10.1016/j.peptides.2012.07.001 1:CAS:528:DC%2BC38XhtlKku7vE
    • Li Y, Qi X, Zhang QH, Huang YD, Su ZJ. Overview on the recent study of antimicrobial peptides: Origins, functions, relative mechanisms and application. Peptides, 2012, 37(2):207-215
    • (2012) Peptides , vol.37 , Issue.2 , pp. 207-215
    • Li, Y.1    Qi, X.2    Zhang, Q.H.3    Huang, Y.D.4    Su, Z.J.5
  • 2
    • 0037050278 scopus 로고    scopus 로고
    • Rozek. Role of membranes in the activities of antimicrobial cationic peptides
    • 10.1111/j.1574-6968.2002.tb11000.x 1:CAS:528:DC%2BD38Xos1Ontg%3D%3D
    • Hancock REW, Rozek. Role of membranes in the activities of antimicrobial cationic peptides. Fems Microbiol Lett, 2002, 206(2):143-149
    • (2002) Fems Microbiol Lett , vol.206 , Issue.2 , pp. 143-149
    • Hancock, R.E.W.1
  • 3
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge require-ments for activity
    • 10.1016/S0005-2736(99)00199-6 1:CAS:528:DyaK1MXnslymurc%3D
    • Sitaram N, Nagaraj R. Interaction of antimicrobial peptides with biological and model membranes: Structural and charge require-ments for activity. Biochimica et biophysica acta, 1999, 1462(1-2):29-54
    • (1999) Biochimica et Biophysica Acta , vol.1462 , Issue.1-2 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 4
    • 34248993592 scopus 로고    scopus 로고
    • Fungicidal effect of pleurocidin by membrane-active mechanism and design of enantiomeric analogue for proteolytic resistance
    • 10.1016/j.bbamem.2007.02.024 1:CAS:528:DC%2BD2sXlvVyjtrs%3D
    • Jung HJ, Park Y, Sung WS, Suh BK, Lee J, Hahm KS, Lee DG. Fungicidal effect of pleurocidin by membrane-active mechanism and design of enantiomeric analogue for proteolytic resistance. Biochim Biophys Acta, 2007, 1768(6):1400-1405
    • (2007) Biochim Biophys Acta , vol.1768 , Issue.6 , pp. 1400-1405
    • Jung, H.J.1    Park, Y.2    Sung, W.S.3    Suh, B.K.4    Lee, J.5    Hahm, K.S.6    Lee, D.G.7
  • 5
    • 34247153326 scopus 로고    scopus 로고
    • Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides
    • 10.1128/AAC.00925-06 1:CAS:528:DC%2BD2sXktlOjtLY%3D
    • Chen Y, Guarnieri MT, Vasil AI, Vasil ML, Mant CT, Hodges RS. Role of peptide hydrophobicity in the mechanism of action of alpha-helical antimicrobial peptides. Antimicrob Agents Chemother, 2007, 51(4):1398-406
    • (2007) Antimicrob Agents Chemother , vol.51 , Issue.4 , 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
    • 84863888013 scopus 로고    scopus 로고
    • Adsorption of antimicrobial indolicidin-derived peptides on hydrophobic surfaces
    • 10.1021/la301401v 1:CAS:528:DC%2BC38XovFaqs70%3D
    • Tsai CW, Ruaan RC, Liu CI. Adsorption of antimicrobial indolicidin-derived peptides on hydrophobic surfaces. Langmuir, 2012, 28(28):10446-10452
    • (2012) Langmuir , vol.28 , Issue.28 , pp. 10446-10452
    • Tsai, C.W.1    Ruaan, R.C.2    Liu, C.I.3
  • 8
    • 0037194346 scopus 로고    scopus 로고
    • Design of novel analogue peptides with potent antibiotic activity based on the antimicrobial peptide, HP (2-20), derived from N-terminus of Helicobacter pylori ribosomal protein L1
    • 1:CAS:528:DC%2BD38XmslKlsLc%3D
    • Lee DG, Kim HN, Park Y, Kim HK, Choi BH, Choi CH, Hahm KS. Design of novel analogue peptides with potent antibiotic activity based on the antimicrobial peptide, HP (2-20), derived from N-terminus of Helicobacter pylori ribosomal protein L1. Biochim Biophys Acta, 2002, 1598(1-2):185-194
    • (2002) Biochim Biophys Acta , vol.1598 , Issue.1-2 , pp. 185-194
    • Lee, D.G.1    Kim, H.N.2    Park, Y.3    Kim, H.K.4    Choi, B.H.5    Choi, C.H.6    Hahm, K.S.7
  • 9
    • 79955748813 scopus 로고    scopus 로고
    • Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework
    • 10.1158/1535-7163.MCT-10-0811 1:CAS:528:DC%2BC3MXivVCku7k%3D
    • Huang YB, Wang XF, Wang HY, Liu Y, Chen Y. Studies on mechanism of action of anticancer peptides by modulation of hydrophobicity within a defined structural framework. Mol Cancer Ther, 2011, 10(3):416-426
    • (2011) Mol Cancer Ther , vol.10 , Issue.3 , pp. 416-426
    • Huang, Y.B.1    Wang, X.F.2    Wang, H.Y.3    Liu, Y.4    Chen, Y.5
  • 10
    • 0035006334 scopus 로고    scopus 로고
    • Proinflammatory activity of a cecropin-like antibacterial peptide from Helicobacter pylori
    • 10.1128/AAC.45.6.1700-1704.2001 1:CAS:528:DC%2BD3MXjslyqs7s%3D
    • Bylund J, Christophe T, Boulay F, Nystrom T, Karlsson A, Dahlgren C. Proinflammatory activity of a cecropin-like antibacterial peptide from Helicobacter pylori. Antimicrob Agents Chemother, 2001, 45(6):1700-1704
    • (2001) Antimicrob Agents Chemother , vol.45 , Issue.6 , pp. 1700-1704
    • Bylund, J.1    Christophe, T.2    Boulay, F.3    Nystrom, T.4    Karlsson, A.5    Dahlgren, C.6
  • 11
    • 0033594420 scopus 로고    scopus 로고
    • Antibacterial peptide from H pylori
    • 10.1038/19439 1:CAS:528:DyaK1MXivVeis78%3D
    • Putsep K, Branden CI, Boman HG, Normark S. Antibacterial peptide from H. pylori. Nature, 1999, 398(6729):671-672
    • (1999) Nature , vol.398 , Issue.6729 , pp. 671-672
    • Putsep, K.1    Branden, C.I.2    Boman, H.G.3    Normark, S.4
  • 12
    • 76049129382 scopus 로고    scopus 로고
    • Structure guided de novo design of alpha-helical antimicrobial peptide with enhanced specificity
    • 10.1351/PAC-CON-09-01-12 1:CAS:528:DC%2BC3cXhvFSjsb0%3D
    • Huang JF, Xu YM, Hao DM, Huang YB, Liu Y, Chen YX. Structure guided de novo design of alpha-helical antimicrobial peptide with enhanced specificity. Pure Appl Chem, 2010, 82(1):243-257
    • (2010) Pure Appl Chem , vol.82 , Issue.1 , pp. 243-257
    • Huang, J.F.1    Xu, Y.M.2    Hao, D.M.3    Huang, Y.B.4    Liu, Y.5    Chen, Y.X.6
  • 13
    • 0036185353 scopus 로고    scopus 로고
    • Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic alpha-helix
    • 10.1046/j.1397-002x.2001.10994.x 1:CAS:528:DC%2BD38XitlSrt7c%3D
    • Chen Y, Mant CT, Hodges RS. Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic alpha-helix. J Pept Res, 2002, 59(1):18-33
    • (2002) J Pept Res , vol.59 , Issue.1 , pp. 18-33
    • Chen, Y.1    Mant, C.T.2    Hodges, R.S.3
  • 14
    • 16844373772 scopus 로고    scopus 로고
    • Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index
    • 10.1074/jbc.M413406200 1:CAS:528:DC%2BD2MXislyht7k%3D
    • Chen Y, Mant CT, Farmer SW, Hancock RE, Vasil ML, Hodges RS. Rational design of alpha-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J Biol Chem, 2005, 280(13):12316-12329
    • (2005) J Biol Chem , vol.280 , Issue.13 , pp. 12316-12329
    • Chen, Y.1    Mant, C.T.2    Farmer, S.W.3    Hancock, R.E.4    Vasil, M.L.5    Hodges, R.S.6
  • 15
    • 0024982236 scopus 로고
    • Effect of preferred binding domains on peptide retention behavior in reversed-phase chromatography: Amphipathic alpha-helices
    • 1:CAS:528:DyaK3cXktlOhsr8%3D
    • Zhou NE, Mant CT, Hodges RS. Effect of preferred binding domains on peptide retention behavior in reversed-phase chromatography: Amphipathic alpha-helices. Pept Res, 1990, 3(1):8-20
    • (1990) Pept Res , vol.3 , Issue.1 , pp. 8-20
    • Zhou, N.E.1    Mant, C.T.2    Hodges, R.S.3
  • 16
    • 33646231485 scopus 로고    scopus 로고
    • Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects
    • 10.1002/bip.20417 1:CAS:528:DC%2BD28Xkt1Gkt7o%3D
    • Kovacs JM, Mant CT, Hodges RS. Determination of intrinsic hydrophilicity/hydrophobicity of amino acid side chains in peptides in the absence of nearest-neighbor or conformational effects. Biopolymers, 2006, 84(3):283-297
    • (2006) Biopolymers , vol.84 , Issue.3 , pp. 283-297
    • Kovacs, J.M.1    Mant, C.T.2    Hodges, R.S.3
  • 17
    • 0038265111 scopus 로고    scopus 로고
    • A novel method to measure self-association of small amphipathic molecules: Temperature profiling in reversed-phase chromatography
    • 10.1074/jbc.M301777200 1:CAS:528:DC%2BD3sXksF2iurk%3D
    • Lee DL, Mant CT, Hodges RS. A novel method to measure self-association of small amphipathic molecules: Temperature profiling in reversed-phase chromatography. J Biol Chem, 2003, 278(25):22918-22927
    • (2003) J Biol Chem , vol.278 , Issue.25 , pp. 22918-22927
    • Lee, D.L.1    Mant, C.T.2    Hodges, R.S.3
  • 18
    • 0043135171 scopus 로고    scopus 로고
    • Temperature profiling of polypeptides in reversed-phase liquid chromatography. I. Monitoring of dimerization and unfolding of amphipathic alpha-helical peptides
    • 1:CAS:528:DC%2BD3sXmsVGqu74%3D
    • Mant CT, Chen Y, Hodges RS. Temperature profiling of polypeptides in reversed-phase liquid chromatography. I. Monitoring of dimerization and unfolding of amphipathic alpha-helical peptides. J Chromatogr A, 2003, 1009(1-2):29-43
    • (2003) J Chromatogr A , vol.1009 , Issue.1-2 , pp. 29-43
    • Mant, C.T.1    Chen, Y.2    Hodges, R.S.3
  • 19
    • 33746532309 scopus 로고    scopus 로고
    • Peptide antimicrobial agents
    • 10.1128/CMR.00056-05 1:CAS:528:DC%2BD28XosVaqsrk%3D
    • Jenssen H, Hamill P, Hancock RE. Peptide antimicrobial agents. Clin Microbiol Rev, 2006, 19(3):491-511
    • (2006) Clin Microbiol Rev , vol.19 , Issue.3 , pp. 491-511
    • Jenssen, H.1    Hamill, P.2    Hancock, R.E.3
  • 20
    • 84865605029 scopus 로고    scopus 로고
    • A review of Candida species causing blood stream infection
    • 10.4103/0255-0857.99484 1:STN:280:DC%2BC38fntlehug%3D%3D
    • Giri S, Kindo AJ. A review of Candida species causing blood stream infection. Indian J Med Microbiol, 2012, 30(3):270-278
    • (2012) Indian J Med Microbiol , vol.30 , Issue.3 , pp. 270-278
    • Giri, S.1    Kindo, A.J.2
  • 21
    • 0037133202 scopus 로고    scopus 로고
    • Conjugation of a magainin analogue with lipophilic acids controls hydrophobicity, solution assembly, and cell selectivity
    • 10.1021/bi011549t 1:CAS:528:DC%2BD38Xnt1GlsA%3D%3D
    • Avrahami D, Shai Y. Conjugation of a magainin analogue with lipophilic acids controls hydrophobicity, solution assembly, and cell selectivity. Biochemistry, 2002, 41(7):2254-2263
    • (2002) Biochemistry , vol.41 , Issue.7 , pp. 2254-2263
    • Avrahami, D.1    Shai, Y.2
  • 22
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/ remodeling of distinct molecular species en route to the plasma membrane
    • 10.1083/jcb.146.4.741 1:CAS:528:DyaK1MXls1Srt70%3D
    • Schneiter R, Brugger B, Sandhoff R, Zellnig G, Leber A, Lampl M, Athenstaedt K, Hrastnik C, Eder S, Daum G, Paltauf F, Wieland FT, Kohlwein SD. Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/ remodeling of distinct molecular species en route to the plasma membrane. J Cell Biol, 1999, 146(4):741-754
    • (1999) J Cell Biol , vol.146 , Issue.4 , pp. 741-754
    • Schneiter, R.1    Brugger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6    Athenstaedt, K.7    Hrastnik, C.8    Eder, S.9    Daum, G.10    Paltauf, F.11    Wieland, F.T.12    Kohlwein, S.D.13
  • 23
    • 33745113451 scopus 로고    scopus 로고
    • Comparison of biophysical and biologic properties of alpha-helical enantiomeric antimicrobial peptides
    • 10.1111/j.1747-0285.2006.00349.x 1:CAS:528:DC%2BD28XktFSht78%3D
    • Chen Y, Vasil AI, Rehaume L, Mant CT, Burns JL, Vasil ML, Hancock RE, Hodges RS. Comparison of biophysical and biologic properties of alpha-helical enantiomeric antimicrobial peptides. Chem Biol Drug Des, 2006, 67(2):162-173
    • (2006) Chem Biol Drug des , vol.67 , Issue.2 , pp. 162-173
    • Chen, Y.1    Vasil, A.I.2    Rehaume, L.3    Mant, C.T.4    Burns, J.L.5    Vasil, M.L.6    Hancock, R.E.7    Hodges, R.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.