Functional regulation of aquaporin dynamics by lipid bilayer composition

Anh T. P. Nguyen, Austin T. Weigle and Diwakar Shukla ()
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Anh T. P. Nguyen: University of Illinois Urbana-Champaign
Austin T. Weigle: University of Illinois Urbana-Champaign
Diwakar Shukla: University of Illinois Urbana-Champaign

Nature Communications, 2024, vol. 15, issue 1, 1-19

Abstract: Abstract With the diversity of lipid-protein interactions, any observed membrane protein dynamics or functions directly depend on the lipid bilayer selection. However, the implications of lipid bilayer choice are seldom considered unless characteristic lipid-protein interactions have been previously reported. Using molecular dynamics simulation, we characterize the effects of membrane embedding on plant aquaporin SoPIP2;1, which has no reported high-affinity lipid interactions. The regulatory impacts of a realistic lipid bilayer, and nine different homogeneous bilayers, on varying SoPIP2;1 dynamics are examined. We demonstrate that SoPIP2;1’s structure, thermodynamics, kinetics, and water transport are altered as a function of each membrane construct’s ensemble properties. Notably, the realistic bilayer provides stabilization of non-functional SoPIP2;1 metastable states. Hydrophobic mismatch and lipid order parameter calculations further explain how lipid ensemble properties manipulate SoPIP2;1 behavior. Our results illustrate the importance of careful bilayer selection when studying membrane proteins. To this end, we advise cautionary measures when performing membrane protein molecular dynamics simulations.

Date: 2024
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DOI: 10.1038/s41467-024-46027-y

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