Interfacial polar interactions affect gramicidin channel kinetics.

Abstract:

:Critical to biological processes such as secretion and transport, protein-lipid interactions within the membrane and at the membrane-water interface still raise many questions. Here we examine the role of lipid headgroups in these interactions by using gramicidin A (gA) channels in planar bilayers as a probe. We show that although headgroup demethylation from phosphatidylcholine (DOPC) to phosphatidylethanolamine decreases the lifetime of gA channels by an order of magnitude in accordance with the currently accepted hydrophobic mismatch mechanism, our findings with diether-DOPC suggest the importance of the headgroup-peptide interactions. According to our x-ray diffraction measurements, this lipid has the same hydrophobic thickness as DOPC but increases gA lifetime by a factor of 2. Thus we demonstrate that peptide-headgroup interactions may dominate over the effect of hydrophobic mismatch in regulating protein function.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Rostovtseva TK,Petrache HI,Kazemi N,Hassanzadeh E,Bezrukov SM

doi

10.1529/biophysj.107.120261

subject

Has Abstract

pub_date

2008-02-15 00:00:00

pages

L23-5

issue

4

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(08)70630-1

journal_volume

94

pub_type

信件
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