More than the sum of its parts: Coarse-grained peptide-lipid interactions from a simple cross-parametrization
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.
The results show that the cross-parametrization can reproduce a number of structural properties of membrane peptides, in agreement with existing peptide-lipid CG force fields, and finds encouraging results for two challenging biophysical problems.
@article{Bereau_2014,
doi = {10.1063/1.4867465},
url = {https://doi.org/10.1063%2F1.4867465},
year = 2014,
month = {mar},
publisher = {{AIP} Publishing},
volume = {140},
number = {11},
author = {Tristan Bereau and Zun-Jing Wang and Markus Deserno},
title = {More than the sum of its parts: Coarse-grained peptide-lipid interactions from a simple cross-parametrization},
journal = {The Journal of Chemical Physics}
}