Conformational analysis of melittin in solution phase: vibrational circular dichroism study.

Wang F, Polavarapu PL
Biopolymers. 2003 70 (4): 614-9

PMID: 14648771 · DOI:10.1002/bip.10504

The vibrational absorption and vibrational circular dichroism (VCD) spectra of melittin in D(2)O solutions at different pH values, different salt concentrations, or different 2,2,2-trifluoroethanol (TFE) concentrations are recorded in the amide I' (1850-1600 cm(-1)) region. Two models are used to simulate this peptide in different conditions, and a coupled oscillator program is used to obtain the calculated absorption and VCD spectra. This study indicates that melittin adopts a mixed structure in D(2)O solution at low pH, low salt concentration, or low TFE concentration. With an increase in pH, salt concentration, or TFE concentration, the structure changes to alpha-helix and further increases lead to aggregation. These results demonstrate the versatility of VCD in probing the conformations of peptides under different environmental perturbations.

Copyright 2003 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 70: 614-619, 2003

MeSH Terms (7)

Circular Dichroism Hydrogen-Ion Concentration Melitten Potassium Chloride Protein Conformation Solutions Trifluoroethanol

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