메뉴 건너뛰기




Volumn 334, Issue 4, 2005, Pages 1329-1335

The role of the central L- or D-Pro residue on structure and mode of action of a cell-selective α-helical IsCT-derived antimicrobial peptide

Author keywords

helical antimicrobial peptide; Bacterial membranes; Cell selectivity; D Pro kink; Intracellular components; IsCT; L Pro kink; Mechanism; Potential depolarization; Structure

Indexed keywords

ANTIINFECTIVE AGENT; ANTIMICROBIAL CATIONIC PEPTIDE; LIPOSOME; PROLINE;

EID: 23044494735     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.07.029     Document Type: Article
Times cited : (26)

References (21)
  • 1
    • 0034255255 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in animal defenses
    • R.E. Hancock, and M.G. Scott The role of antimicrobial peptides in animal defenses Proc. Natl. Acad. Sci. USA 97 2000 8856 8861
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8856-8861
    • Hancock, R.E.1    Scott, M.G.2
  • 2
    • 0034283216 scopus 로고    scopus 로고
    • The role of cationic antimicrobial peptides in innate host defences
    • R.E. Hancock, and G. Diamond The role of cationic antimicrobial peptides in innate host defences Trends Microbiol. 8 2000 402 410
    • (2000) Trends Microbiol. , vol.8 , pp. 402-410
    • Hancock, R.E.1    Diamond, G.2
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 4
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: An overview
    • D. Andreu, and L. Rivas Animal antimicrobial peptides: an overview Biopolymers 47 1998 415 433
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 5
    • 0033864862 scopus 로고    scopus 로고
    • Amphipathic, α-helical antimicrobial peptides
    • A. Tossi, L. Sandri, and A. Giangaspero Amphipathic, α-helical antimicrobial peptides Biopolymers 55 2000 4 30
    • (2000) Biopolymers , vol.55 , pp. 4-30
    • Tossi, A.1    Sandri, L.2    Giangaspero, A.3
  • 6
    • 0033485640 scopus 로고    scopus 로고
    • Structural and functional implications of a proline residue in the antimicrobial peptide gaegurin
    • J.Y. Suh, Y.T. Lee, C.B. Park, K.H. Lee, S.C. Kim, and B.S. Choi Structural and functional implications of a proline residue in the antimicrobial peptide gaegurin Eur. J. Biochem. 266 1999 665 674
    • (1999) Eur. J. Biochem. , vol.266 , pp. 665-674
    • Suh, J.Y.1    Lee, Y.T.2    Park, C.B.3    Lee, K.H.4    Kim, S.C.5    Choi, B.S.6
  • 8
    • 0036295702 scopus 로고    scopus 로고
    • Structural studies of porcine myeloid antibacterial peptide PMAP-23 and its analogues in DPC micelles by NMR spectroscopy
    • K. Park, D. Oh, S.Y. Shin, K.-S. Hahm, and Y. Kim Structural studies of porcine myeloid antibacterial peptide PMAP-23 and its analogues in DPC micelles by NMR spectroscopy Biochem. Biophys. Res. Commun. 290 2002 204 212
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 204-212
    • Park, K.1    Oh, D.2    Shin, S.Y.3    Hahm, K.-S.4    Kim, Y.5
  • 9
    • 0942279702 scopus 로고    scopus 로고
    • Investigating the importance of the flexible hinge in caerin 1.1: Solution structures and activity of two synthetically modified caerin peptides
    • T.L. Pukala, C.S. Brinkworth, J.A. Carver, and J.H. Bowie Investigating the importance of the flexible hinge in caerin 1.1: solution structures and activity of two synthetically modified caerin peptides Biochemistry 43 2004 937 944
    • (2004) Biochemistry , vol.43 , pp. 937-944
    • Pukala, T.L.1    Brinkworth, C.S.2    Carver, J.A.3    Bowie, J.H.4
  • 10
    • 0033594986 scopus 로고    scopus 로고
    • Influence of proline residues on the antibacterial and synergistic activities of α-helical peptides
    • L. Zhang, R. Benz, and R.E. Hancock Influence of proline residues on the antibacterial and synergistic activities of α-helical peptides Biochemistry 38 1999 8102 8111
    • (1999) Biochemistry , vol.38 , pp. 8102-8111
    • Zhang, L.1    Benz, R.2    Hancock, R.E.3
  • 11
    • 0034601806 scopus 로고    scopus 로고
    • Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures
    • D. Oh, S.Y. Shin, S. Lee, J.H. Kang, S.D. Kim, P.D. Ryu, K.-S. Hahm, and Y. Kim Role of the hinge region and the tryptophan residue in the synthetic antimicrobial peptides, cecropin A(1-8)-magainin 2(1-12) and its analogues, on their antibiotic activities and structures Biochemistry 39 2000 11855 11864
    • (2000) Biochemistry , vol.39 , pp. 11855-11864
    • Oh, D.1    Shin, S.Y.2    Lee, S.3    Kang, J.H.4    Kim, S.D.5    Ryu, P.D.6    Hahm, K.-S.7    Kim, Y.8
  • 12
    • 0347635410 scopus 로고    scopus 로고
    • Effects of l- or d-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic alpha-helical model peptide on structure and cell selectivity
    • Y.M. Song, S.T. Yang, S.S. Lim, Y. Kim, K.-S. Hahm, J.I. Kim, and S.Y. Shin Effects of l- or d-Pro incorporation into hydrophobic or hydrophilic helix face of amphipathic alpha-helical model peptide on structure and cell selectivity Biochem. Biophys. Res. Commun. 314 2004 615 621
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 615-621
    • Song, Y.M.1    Yang, S.T.2    Lim, S.S.3    Kim, Y.4    Hahm, K.-S.5    Kim, J.I.6    Shin, S.Y.7
  • 13
    • 4544349379 scopus 로고    scopus 로고
    • Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs
    • K. Lee, S.Y. Shin, K. Kim, S.S. Lim, K.-S. Hahm, and Y. Kim Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs Biochem. Biophys. Res. Commun. 323 2004 712 719
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 712-719
    • Lee, K.1    Shin, S.Y.2    Kim, K.3    Lim, S.S.4    Hahm, K.-S.5    Kim, Y.6
  • 15
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • A.I. De Kroon, M.W. Soekarjo, J. De Gier, and B. De Kruijff The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers Biochemistry 29 1990 8229 8240
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • De Kroon, A.I.1    Soekarjo, M.W.2    De Gier, J.3    De Kruijff, B.4
  • 16
    • 0037067706 scopus 로고    scopus 로고
    • Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence
    • H. Zhao, and P.K. Kinnunen Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence J. Biol. Chem. 277 2002 25170 25177
    • (2002) J. Biol. Chem. , vol.277 , pp. 25170-25177
    • Zhao, H.1    Kinnunen, P.K.2
  • 17
    • 0033915369 scopus 로고    scopus 로고
    • Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria
    • C.L. Friedrich, D. Moyles, T.J. Beveridge, and R.E. Hancock Antibacterial action of structurally diverse cationic peptides on gram-positive bacteria Antimicrob. Agents Chemother. 44 2000 2086 2092
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2086-2092
    • Friedrich, C.L.1    Moyles, D.2    Beveridge, T.J.3    Hancock, R.E.4
  • 18
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • Y. Shai, and Z. Oren From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides Peptides 22 2001 1629 1641
    • (2001) Peptides , vol.22 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 19
    • 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
    • C.B. Park, H.S. Kim, and S.C. Kim 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. 244 1998 253 257
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 20
    • 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
    • C.B. Park, K.S. Yi, K. Matsuzaki, M.S. Kim, and S.C. Kim 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 97 2000 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
  • 21
    • 0034713613 scopus 로고    scopus 로고
    • Interactions of the novel antimicrobial peptide buforin2 with lipid bilayers: Proline as a translocation promoting factor
    • S. Kobayashi, K. Takeshima, C.B. Park, S.C. Kim, and K. Matsuzaki Interactions of the novel antimicrobial peptide buforin2 with lipid bilayers: proline as a translocation promoting factor Biochemistry 39 2000 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.