Issue 32, 2022

Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?

Abstract

Simulating the process of amyloid aggregation with atomic detail is a challenging task for various reasons. One of them is that it is difficult to parametrise a force field such that all protein states ranging from the folded through the unfolded to the aggregated state are represented with the same level of accuracy. Here, we test whether the consideration of electronic polarisability improves the description of the different states of Aβ16–22. Surprisingly, the CHARMM Drude polarisable force field is found to perform worse than its unpolarisable counterpart CHARMM36m. Sources for this failure of the Drude model are discussed.

Graphical abstract: Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?

Supplementary files

Article information

Article type
Paper
Submitted
06 Marts 2022
Accepted
11 Jūl. 2022
First published
21 Jūl. 2022
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2022,12, 20829-20837

Does the inclusion of electronic polarisability lead to a better modelling of peptide aggregation?

B. Kav and B. Strodel, RSC Adv., 2022, 12, 20829 DOI: 10.1039/D2RA01478E

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