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The 11‐mer repeats of human α‐synuclein in vesicle interactions and lipid composition discrimination: A cooperative role
Author(s) -
Bisaglia Marco,
Schievano Elisabetta,
Caporale Andrea,
Peggion Evaristo,
Mammi Stefano
Publication year - 2006
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20440
Subject(s) - chemistry , vesicle , phospholipid , composition (language) , amphiphile , sequence (biology) , biochemistry , biophysics , membrane , biology , polymer , copolymer , philosophy , linguistics , organic chemistry
α‐Synuclein is a protein abundant in presynaptic terminals in the brain. The N‐terminal region of the sequence contains an imperfect 11‐residue periodicity also found in A‐class apolipoproteins and able to fold into an amphipathic helix. Here, the ability of three fragments of the protein, which include one, two, and all repeats, respectively, to bind to vesicles of different phospholipid composition is described. The results suggest a cooperative action of the repeats in selecting target membranes for interaction based on their lipid composition. This deduction is possibly related to the physiological role of the protein, which is still poorly understood. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 84: 310–316, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com