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

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.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Ivanova VP,Makarov IM,Schäffer TE,Heimburg T

doi

10.1016/S0006-3495(03)75047-4

subject

Has Abstract

pub_date

2003-04-01 00:00:00

pages

2427-39

issue

4

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(03)75047-4

journal_volume

84

pub_type

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