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The 11-mer repeats of human alpha-synuclein in vesicle interactions and lipid composition discrimination: a cooperative role.
- Source :
-
Biopolymers [Biopolymers] 2006; Vol. 84 (3), pp. 310-6. - Publication Year :
- 2006
-
Abstract
- alpha-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.<br /> (Copyright 2006 Wiley Periodicals, Inc.)
- Subjects :
- Amino Acid Sequence
Amino Acids chemistry
Circular Dichroism
Humans
Liposomes chemistry
Liposomes metabolism
Models, Molecular
Phospholipids chemistry
Phospholipids metabolism
Protein Binding
Protein Structure, Secondary
Spectrophotometry, Ultraviolet
Lipid Metabolism
alpha-Synuclein chemistry
alpha-Synuclein metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3525
- Volume :
- 84
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biopolymers
- Publication Type :
- Academic Journal
- Accession number :
- 16411187
- Full Text :
- https://doi.org/10.1002/bip.20440