期刊
JOURNAL OF CHEMICAL PHYSICS
卷 140, 期 11, 页码 -出版社
AIP Publishing
DOI: 10.1063/1.4867465
关键词
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资金
- National Institutes of Health (NIH) [P01AG032131]
- Astrid and Bruce McWilliams Fellowship
Interfacial systems are at the core of fascinating phenomena in many disciplines, such as biochemistry, soft-matter physics, and food science. However, the parametrization of accurate, reliable, and consistent coarse-grained (CG) models for systems at interfaces remains a challenging endeavor. In the present work, we explore to what extent two independently developed solvent-free CG models of peptides and lipids-of different mapping schemes, parametrization methods, target functions, and validation criteria-can be combined by only tuning the cross-interactions. Our results show that the cross-parametrization can reproduce a number of structural properties of membrane peptides (for example, tilt and hydrophobic mismatch), in agreement with existing peptide-lipid CG force fields. We find encouraging results for two challenging biophysical problems: (i) membrane pore formation mediated by the cooperative action of several antimicrobial peptides, and (ii) the insertion and folding of the helix-forming peptide WALP23 in the membrane. (C) 2014 AIP Publishing LLC.
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