Functional regulation of aquaporin dynamics by lipid bilayer composition.

Autor: Nguyen ATP; Department of Chemical and Biomolecular Engineering, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA., Weigle AT; Department of Chemistry, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA., Shukla D; Department of Chemical and Biomolecular Engineering, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA. diwakar.shukla@shuklagroup.org.; Center for Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA. diwakar.shukla@shuklagroup.org.; Department of Bioengineering, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA. diwakar.shukla@shuklagroup.org.; Department of Plant Biology, University of Illinois Urbana-Champaign, Urbana, IL, 61801, USA. diwakar.shukla@shuklagroup.org.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2024 Feb 28; Vol. 15 (1), pp. 1848. Date of Electronic Publication: 2024 Feb 28.
DOI: 10.1038/s41467-024-46027-y
Abstrakt: 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.
(© 2024. The Author(s).)
Databáze: MEDLINE
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