The 11-mer repeats of human α-synuclein in vesicle interactions and lipid composition discrimination:: A cooperative role

被引:29
作者
Bisaglia, M [1 ]
Schievano, E [1 ]
Caporale, A [1 ]
Peggion, E [1 ]
Mammi, S [1 ]
机构
[1] Univ Padua, CNR, Inst Biomol Chem, Dept Chem Sci, I-35131 Padua, Italy
关键词
alpha-synuclein; amphipathic helix; alpha; 11/3-helix; phospholipid vesicles; circular dichroism;
D O I
10.1002/bip.20440
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
alpha-Synuclein is a protein abundant in presynaptic terminals in the brain. Die N-terminal region of the sequence contains an imperfect 11-residue periodicity also found in A-class apolipo-proteins 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 repeals in selecting tat-get 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. (c) 2006 Wiley Periodicals, Inc. Biopolymers
引用
收藏
页码:310 / 316
页数:7
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