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 Jjournal_title
Biophysical journalauthors
Ivanova VP,Makarov IM,Schäffer TE,Heimburg Tdoi
10.1016/S0006-3495(03)75047-4subject
Has Abstractpub_date
2003-04-01 00:00:00pages
2427-39issue
4eissn
0006-3495issn
1542-0086pii
S0006-3495(03)75047-4journal_volume
84pub_type
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