메뉴 건너뛰기




Volumn 17, Issue 11, 2010, Pages 1345-1350

A differential scanning calorimetry study of the effects and interactions of antimicrobial peptide LS3 on phosphatidylethanolamine bilayers

Author keywords

Amphipathic helix; Antimicrobial peptide; DSC; LS3; Phase transition; Phosphatidylethanolamine

Indexed keywords


EID: 78650633261     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866511009011345     Document Type: Article
Times cited : (1)

References (11)
  • 1
    • 0024515763 scopus 로고
    • Protein design, a minimalist approach
    • Review.
    • Degrado, W.F.; Lear, J.D. Protein design, a minimalist approach. Science, 1989, 12, 622-628 Review.
    • (1989) Science , vol.12 , pp. 622-628
    • Degrado, W.F.1    Lear, J.D.2
  • 2
    • 0026721333 scopus 로고
    • Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesicles
    • Chung, L.A.; Lear, J.D.; DeGrado, W.F. Fluorescence studies of the secondary structure and orientation of a model ion channel peptide in phospholipid vesicles. Biochemistry, 1992, 31, 6608-6616.
    • (1992) Biochemistry , vol.31 , pp. 6608-6616
    • Chung, L.A.1    Lear, J.D.2    Degrado, W.F.3
  • 3
    • 0030974351 scopus 로고    scopus 로고
    • Electrostatic effects on ion selectivity and rectification in designed ion channel peptides
    • Lear, J. D.; Schneider, J. P.; Kienker, P. K.; De Grado, W. F. Electrostatic effects on ion selectivity and rectification in designed ion channel peptides. J. Am. Chem. Soc., 1997, 119, 3212-3217.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3212-3217
    • Lear, J.D.1    Schneider, J.P.2    Kienker, P.K.3    De Grado, W.F.4
  • 6
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • Nath, A.; Atkins, W. M.; Sligar, S. G. Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry, 2007, 46, 2059-2069.
    • (2007) Biochemistry , vol.46 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 8
    • 0038778549 scopus 로고    scopus 로고
    • Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation
    • Chen, F.; Lee, M.; Huang, H. W. Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Bio-phys. J., 2003, 84, 3751-8.
    • (2003) Bio-phys. J. , vol.84 , pp. 3751-3758
    • Chen, F.1    Lee, M.2    Huang, H.W.3
  • 9
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht, T.; Dathe, M.; Epand, R. M.; Beyermann, M.; Krause, E.; Maloy, W. L.; MacDonald, D. L.; Bienert, M. Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry, 1997, 36, 12869-80.
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyermann, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 10
    • 0034713831 scopus 로고    scopus 로고
    • Current action of antimicrobial peptides: Two-state model
    • Huang, H. W. Current action of antimicrobial peptides: two-state model. Biochemistry, 2000, 39, 8347-8352.
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 11
    • 0031006189 scopus 로고    scopus 로고
    • Effect of changing the size of lipid headgroup on peptide insertion into membranes
    • Heller, W.; He, K., Ludtke, S.; Harroun, T.; and Huang, H. Effect of changing the size of lipid headgroup on peptide insertion into membranes. Biophys. J., 1997, 73, 239-244.
    • (1997) Biophys. J. , vol.73 , pp. 239-244
    • Heller, W.1    He Ludtke, K.S.2    Harroun, T.3    Huang, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.