1 Department of Ophthalmology, Faculty of Medicine , Université Laval , Quebec City , QC G1V 0A6 , Canada.
2 CUO-Recherche, Centre de Recherche du CHU de Québec, Hôpital du Saint-Sacrement , CHU de Québec , Quebec City , G1S 4L8 , Canada.
3 Department of Chemistry, Faculty of Sciences , Université du Québec à Montréal , Montreal , H2X 2J6 , Canada.
4 Department of Chemistry and Biochemistry and Centre for NanoScience Research , Concordia University , Montreal , H4B 1R6 , Canada.
5 UMR 7099, CNRS-Université Paris Diderot, Institut de Biologie Physico-Chimique , Paris 75005 , France.

AHNAK C-Terminal Peptide Membrane Binding-Interactions between the Residues 5654-5673 of AHNAK and Phospholipid Monolayers and Bilayers.

Langmuir. 2020 01 14; 36(1):362-369

Authors: Yan X, Noël F, Marcotte I, DeWolf CE, Warschawski DE, Boisselier E

Abstract

The dysferlin membrane repair complex contains a small complex, S100A10-annexin A2, which initiates membrane repair by recruiting the protein AHNAK to the membrane, where it interacts via binding sites in the C-terminal region. However, no molecular data are available for the membrane binding of the various proteins involved in this complex. Therefore, the present study investigated the membrane binding of AHNAK to elucidate its role in the cell membrane repair process. A chemically synthesized peptide (pAHNAK), comprising the 20 amino acids in the C-terminal domain of AHNAK, was applied to Langmuir monolayer models, and the binding parameters and insertion angles were measured with surface tensiometry and ellipsometry. The interaction of pAHNAK with lipid bilayers was studied using 31P solid-state nuclear magnetic resonance. pAHNAK preferentially and strongly interacted with phospholipids that comprised negatively charged polar head groups with unsaturated lipids. This finding provides a better understanding of AHNAK membrane behavior and the parameters that influence its function in membrane repair.

PMID: 31825630 [PubMed - indexed for MEDLINE]