Polar angle as a determinant of amphipathic α-helix-lipid interactions: A model peptide study

Biophysical Journal

Volumn 79, Issue 4, 2000, Pages 2075-2083

  Uematsu, Natsuko ^a   Matsuzaki, Katsumi ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT; SYNTHETIC PEPTIDE;

ARTICLE; BILAYER MEMBRANE; CIRCULAR DICHROISM; DRUG SYNTHESIS; LIPID BILAYER; MEMBRANE PERMEABILITY; NONHUMAN; PEPTIDE SYNTHESIS; PROTEIN LIPID INTERACTION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;

EID: 0033799243     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76455-1     Document Type: Article

References (11)

1. Bartlett, G. R. 1959. Phosphorus assay in column chromatography. J. Biol. Chem. 234:466-468.
2. Bechinger, B. 1999. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim. Biophys. Acta. 1462:157-183.
3. Blondelle, S. E., and R. A. Houghten. 1992. Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry. 31:12688-12694.
4. Dathe, M., M. Schümann, T. Wieprecht, A. Winkler, K. Matsuzaki, O. Murase, M. Beyermann, E. Krause, and M. Bienert. 1996. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry: 35:12612-12622.
5. Dathe, M., T. Wieprecht, H. Nikolenko, L. Handel, W. L. Maloy, D. L. MacDonald, M. Beyermann, and M. Bienert. 1997. Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett. 403:208-212.
6. Deisenhofer, J., and H. Michel. 1989. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. EMBO J. 8:2149-2170.
7. Matsuzaki, K., M. Harada, S. Funakoshi, N. Fujii, and K. Miyajima. 1991. Physicochemical determinants for the interactions of magainins 1 and 2 with acidic lipid bilayers. Biochim. Biophys. Acta. 1063:162-170.
8. Matsuzaki, K., Y. Mitani, K. Akada, O. Murase, S. Yoneyama, M. Zasloff, and K. Miyajima. 1998a. Mechanism of synergism between antimicrobial peptides magainin 2 and PGLa. Biochemistry. 37:15144-15153.
9. Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1995a. Translocation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore. Biochemistry. 34:6521-6526.
10. Matsuzaki, K., O. Murase, N. Fujii, and K. Miyajima. 1996a. An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry. 35:11361-11368.
11. Zasloff, M. 1987. 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. 84:5449-5453.