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The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel
KTH, Centra, Science for Life Laboratory, SciLifeLab. KTH, Skolan för teknikvetenskap (SCI), Teoretisk fysik, Beräkningsbiofysik.ORCID-id: 0000-0002-3364-6647
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2016 (engelsk)Inngår i: PloS Computational Biology, ISSN 1553-734X, E-ISSN 1553-7358, Vol. 12, nr 1, artikkel-id e1004704Artikkel i tidsskrift (Fagfellevurdert) Published
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Abstract [en]

Voltage-gated potassium (K-V) channels are membrane proteins that respond to changes in membrane potential by enabling K+ ion flux across the membrane. Polyunsaturated fatty acids (PUFAs) induce channel opening by modulating the voltage-sensitivity, which can provide effective treatment against refractory epilepsy by means of a ketogenic diet. While PUFAs have been reported to influence the gating mechanism by electrostatic interactions to the voltage-sensor domain (VSD), the exact PUFA-protein interactions are still elusive. In this study, we report on the interactions between the Shaker K-V channel in open and closed states and a PUFA-enriched lipid bilayer using microsecond molecular dynamics simulations. We determined a putative PUFA binding site in the open state of the channel located at the protein-lipid interface in the vicinity of the extracellular halves of the S3 and S4 helices of the VSD. In particular, the lipophilic PUFA tail covered a wide range of non-specific hydrophobic interactions in the hydrophobic central core of the protein-lipid interface, while the carboxylic head group displayed more specific interactions to polar/charged residues at the extracellular regions of the S3 and S4 helices, encompassing the S3-S4 linker. Moreover, by studying the interactions between saturated fatty acids (SFA) and the Shaker K-V channel, our study confirmed an increased conformational flexibility in the polyunsaturated carbon tails compared to saturated carbon chains, which may explain the specificity of PUFA action on channel proteins.

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PLOS , 2016. Vol. 12, nr 1, artikkel-id e1004704
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URN: urn:nbn:se:kth:diva-183220DOI: 10.1371/journal.pcbi.1004704ISI: 000369366100033Scopus ID: 2-s2.0-84956717094OAI: oai:DiVA.org:kth-183220DiVA, id: diva2:908867
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QC 20160303

Tilgjengelig fra: 2016-03-03 Laget: 2016-03-03 Sist oppdatert: 2018-01-10bibliografisk kontrollert

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