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Biophys J. 2003 Apr;84(4):2427-39.

Analyzing heat capacity profiles of peptide-containing membranes: cluster formation of gramicidin A.

Author information

1
Membrane Biophysics and Thermodynamics Group, Max-Planck-Institute for Biophysical Chemistry, 37070 Göttingen, Germany.

Abstract

The analysis of peptide and protein partitioning in lipid membranes is of high relevance for the understanding of biomembrane function. We used statistical thermodynamics analysis to demonstrate the effect of peptide mixing behavior on heat capacity profiles of lipid membranes with the aim to predict peptide aggregation from c(P)-profiles. This analysis was applied to interpret calorimetric data on the interaction of the antibiotic peptide gramicidin A with lipid membranes. The shape of the heat capacity profiles was found to be consistent with peptide clustering in both gel and fluid phase. Applying atomic force microscopy, we found gramicidin A aggregates and established a close link between thermodynamics data and microscopic imaging. On the basis of these findings we described the effect of proteins on local fluctuations. It is shown that the elastic properties of the membrane are influenced in the peptide environment.

PMID:
12668450
PMCID:
PMC1302808
DOI:
10.1016/S0006-3495(03)75047-4
[Indexed for MEDLINE]
Free PMC Article

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