The 11-mer repeats of human α-synuclein in vesicle interactions and lipid composition discrimination: A cooperative role
✍ Scribed by Marco Bisaglia; Elisabetta Schievano; Andrea Caporale; Evaristo Peggion; Stefano Mammi
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2006
- Tongue
- English
- Weight
- 266 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
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 [email protected]