Abstract
Cholesterol and saturated fatty acid stabilize dimerization of helical transmembrane peptides by lowering energy cost related to peptides desolvation from lipids upon dimerization: an insight from atomistic simulation
Highlights
Dietary fatty acids (FAs) are incorporated into phospholipids of cell membranes and influence cellular functions [1,2]
Polyunsaturated FAs (PUFAs) including n-3 PUFAs such as eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) have been shown to inhibit T cell proliferation [5,6], whereas diets rich in saturated FAs have been implicated in the development of metabolic diseases, insulin resistance and atherosclerosis, in which low-grade inflammation is considered to be involved [7]
Shaikh et al reported that saturated FAs-enriched diets increased T cell receptor nanoscale clustering in murine CD4+ T cells to a level usually seen on activated cells, whereas diets enriched in monounsaturated FAs or n-3 PUFA showed no such effect [9]
Summary
Dietary fatty acids (FAs) are incorporated into phospholipids of cell membranes and influence cellular functions [1,2]. Raft-like bilayer stabilizes dimerized state of poly-Ile TM helical peptides To analyze the effect of lipid composition on peptide dimerization propensity, we performed UA simulations totaling 42 micro-seconds of the two identical poly-Ile peptides placed, in bilayers, at varied distances (separations) using umbrella-sampling methods (Figure 1) and obtained the profile of self-dimerization potential of mean force (PMF) (Figure 2).
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