Molecular dynamics simulations of antimicrobial peptides: From membrane binding to trans-membrane channels
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 th...
Saved in:
Published in | INT J QUANTUM CHEM Vol. 83; no. 3-4; pp. 166 - 179 |
---|---|
Main Authors | , |
Format | Journal Article Conference Proceeding |
Language | English |
Published |
New York
John Wiley & Sons, Inc
2001
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | 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 |
---|---|
Bibliography: | ark:/67375/WNG-XFLT44CM-3 ArticleID:QUA1208 NWO/CW/Unilever Welcome Trust istex:B273CC3410E5063ADBCA1424C34A52F199CB9CB6 SourceType-Books-1 ObjectType-Book-1 content type line 25 ObjectType-Conference-2 SourceType-Conference Papers & Proceedings-2 |
ISSN: | 0020-7608 1097-461X |
DOI: | 10.1002/qua.1208 |