Abstract
Be straight to better coordinate two -- Head groups and extended acyl chains of raft-like bilayer lipids can localize in groove between dimerized transmembrane helical peptides and assist sequence-nonspecific stabilization of peptide dimers by cholesterol
Highlights
It has been widely accepted that dimerization or multimerization of transmembrane (TM) domains of membrane proteins plays important roles in regulations of signal transduction
Our recent simulations showed that the lipid raft-like bilayer (1:1:1 POPC/DPPC/cholesterol bilayer) stabilizes the dimeric state of the poly-Ile model peptide (Ile)21 compared to the DOPC bilayer [6]
In the former bilayer, POPC and DPPC molecules were the lipid species that were directly contacting with the peptides, whereas the atoms of cholesterol were seldom located within 3Å from the peptide surface
Summary
It has been widely accepted that dimerization or multimerization of transmembrane (TM) domains of membrane proteins plays important roles in regulations of signal transduction. Recent studies on single-pass receptor proteins have elucidated that dimerization of TM domains is a prerequisite step for receptor activation, activation has been shown in many cases to require further structural changes after dimerization [1,2]. Compared to specific interactions such as those between cholesterol and cholesterolrecognizing peptide motifs [4], sequence-nonspecific effects of cholesterol and FAs on peptide dimerization have been addressed in a limited number of studies. Sequence-nonspecific effects could be important to set the basal activities of receptor proteins, thereby adjusting the tone of cellular activities such as intensity of inflammation [3]. Yano et al [5] showed that homodimer of a helical peptide with a sequence of (AALALAA) is stabilized in a 7:3 POPC/cholesterol bilayer compared to the POPC bilayer
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