Folding of amphipathic α-helices on membranes: Energetics of helix formation by melittin

Journal of Molecular Biology

Volumn 285, Issue 4, 1999, Pages 1363-1369

  Ladokhin, Alexey S ^a   White, Stephen H ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Circular dichroism; Folding energetics; Free energy of transfer; Membrane protein folding; Peptide membrane interactions

Indexed keywords

MELITTIN; MEMBRANE PROTEIN; PHOSPHORYLCHOLINE;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; DIASTEREOISOMER; HYDROGEN BOND; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

APOIDEA;

EID: 0033613815     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2346     Document Type: Article

References (30)

1. Beschiaschvili G., Baeuerle H.-D. Effective charge of melittin upon interaction with POPC vesicles. Biochim. Biophys. Acta. 1068:1991;195-200.
2. Bevins C. L., Zasloff M. Peptides from frog skin. Annu. Rev. Biochem. 59:1990;395-414.
3. Dempsey C. E. The actions of melittin on membranes. Biochim. Biophys. Acta. 1031:1990;143-161.
4. Dempsey C. E., Butler G. S. Helical structure and orientation of melittin in dispersed phospholipid membranes from amide exchange analysis in situ. Biochemistry. 31:1992;11973-11977.
5. Eisenberg D., Schwarz E., Komaromy M., Wall R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:1984;125-142.
6. Greenfield N., Fasman G. D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 8:1969;4108-4116.
7. Hirota N., Mizuno K., Goto Y. Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins. J. Mol. Biol. 275:1998;365-378.
8. Kaiser E. T., Kezdy F. J. Secondary structures of proteins and peptides in amphiphilic environments (a review). Proc. Natl Acad. Sci. USA. 80:1983;1137-1143.
9. Kaiser E. T., Kezdy F. J. Amphiphilic secondary structure: design of peptide hormones. Science. 223:1984;249-255.
10. Kuchinka E., Seelig J. Interaction of melittin with phosphatidylcholine membranes. Binding isotherm and lipid head-group conformation. Biochemistry. 28:1989;4216-4221.
11. Ladokhin A. S., Selsted M. E., White S. H. Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophys. J. 72:1997;794-805.
12. Luo P. Z., Baldwin R. L. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry. 36:1997;8413-8421.
13. Maloy W. L., Kari U. P. Structure-activity studies on magainins and other host defense peptides. Biopolymers. 37:1995;105-122.
14. Mayer L. D., Hope M. J., Cullis P. R. Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim. Biophys. Acta. 858:1986;161-168.
15. Oren Z., Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry. 36:1997;1826-1835.
16. Rohl C. A., Baldwin R. L. Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides. Biochemistry. 36:1997;8435-8442.
17. Schwarz G., Beschiaschvili G. Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer. Biochim. Biophys. Acta. 979:1989;82-90.
18. Schwyzer R. Conformations and orientations of amphiphilic peptides induced by artificial lipid membranes: correlations with biological activity. Chemtracts-Biochem. Mol. Biol. 3:1992;347-379.
19. Shalongo W., Stellwagen E. Dichroic statistical model for prediction and analysis of peptide helicity. Proteins: Struct. Funct. Genet. 28:1997;467-480.
20. Smith R., Separovic F., Milne T. J., Whittaker A., Bennett F. M., Cornell B. A., Makriyannis A. Structure and orientation of the pore-forming peptide, melittin, in lipid bilayers. J. Mol. Biol. 241:1994;456-466.
21. Vogel H. Incorporation of melittin into phosphatidylcholine bilayers: study of binding and conformational changes. FEBS Letters. 134:1981;37-42.
22. Wenk M. R., Seelig J. Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation. Biochemistry. 37:1998;3909-3916.
23. White S. H., Wimley W. C. Peptides in lipid bilayers: structural and thermodynamic basis for partitioning and folding. Curr. Opin. Struct. Biol. 4:1994;79-86.
24. White S. H., Wimley W. C. Hydrophobic interactions of peptides with membrane interfaces. Biochim. Biophys. Acta. 1376:1998;339-352.
25. White S. H., Wimley W. C., Ladokhin A. S., Hristova K. Protein folding in membranes: determining the energetics of peptide-bilayer interactions. Methods Enzymol. 295:1998;62-87.
26. Wieprecht T., Dathe M., Beyermann M., Krause E., Maloy W. L., MacDonald D. L., Bienert M. Peptide hydrophobicity controls the activity and selectivity of magainin 2 amide in interaction with membranes. Biochemistry. 36:1997;6124-6132.
27. Wimley W. C., White S. H. Quantitation of electrostatic and hydrophobic membrane interactions by equilibrium dialysis and reverse-phase HPLC. Anal. Biochem. 213:1993;213-217.
28. Wimley W. C., White S. H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nature Struct. Biol. 3:1996;842-848.
29. Wimley W. C., Hristova K., Ladokhin A. S., Silvestro L., Axelsen P. H., White S. H. Folding of β-sheet membrane proteins: a hydrophobic hexapeptide model. J. Mol. Biol. 277:1998;1091-1110.
30. Wu C.-S., Ikeda K., Yang J. T. Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry. 20:1981;566-570.