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Molecular dynamics simulations of antimicrobial peptides: From membrane binding to trans‐membrane channels
Author(s) -
Tieleman D. P.,
Sansom M. S. P.
Publication year - 2001
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.1208
Subject(s) - alamethicin , membrane , antimicrobial peptides , molecular dynamics , chemistry , ion channel , peptide , biophysics , membrane biophysics , ion , dynamics (music) , membrane protein , lipid bilayer , biochemistry , computational chemistry , physics , biology , organic chemistry , receptor , acoustics
Using a combination of simulations of alamethicin and other antimicrobial peptides in different environments, we discuss a number of pertinent problems in the biophysics of peptide–lipid interactions and ion channels. Molecular dynamics simulations can be used to obtain detailed information about the structure and dynamics of peptides in membrane environments. Such simulations have yielded interesting information on the dynamics of membrane proteins and of water and ions in ion channels. However, reliably simulating binding to membranes, insertion into membranes, and aggregation of peptides both in and at the surface of membranes remain challenging problems. © 2001 John Wiley & Sons, Inc. Int J Quant Chem 83: 166–179, 2001