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Simulation of Peptides at Aqueous InterfacesBehavior of peptides at water-membrane interfaces is of great interest in studies on cellular transport and signaling, membrane fusion, and the action of toxins and antibiotics. Many peptides, which exist in water only as random coils, can form sequence-dependent, ordered structures at aqueous interfaces, incorporate into membranes and self-assembly into functional units, such as simple ion channels. Multi -nanosecond molecular dynamics simulations have been carried out to study the mechanism and energetics of interfacial folding of both non-polar and amphiphilic peptides, their insertion into membranes and association into higher-order structures. The simulations indicate that peptides fold non-sequentially, often through a series of amphiphilic intermediates. They further incorporate into the membrane in a preferred direction as folded monomers, and only then aggregate into dimers and, possibly, further into "dimers of dimers".
Document ID
Document Type
Conference Paper
Pohorille, Andrew (NASA Ames Research Center Moffett Field, CA United States)
Wilson, M. (NASA Ames Research Center Moffett Field, CA United States)
Chipot, C. (NASA Ames Research Center Moffett Field, CA United States)
DeVincenzi, Donald L.
Date Acquired
August 20, 2013
Publication Date
January 1, 2001
Subject Category
Life Sciences (General)
Meeting Information
American Chemical Society Meeting(San Diego, CA)
Funding Number(s)
PROJECT: RTOP 344-38-22-06
Distribution Limits
Work of the US Gov. Public Use Permitted.