The 11-mer repeats of human α-synuclein in vesicle interactions and lipid composition discrimination:: A cooperative role
The 11-mer repeats of human α-synuclein in vesicle interactions and lipid composition discrimination:: A cooperative role
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DOI：
10.1002/bip.20440
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发表时间：
2006-01-01
期刊：
影响因子：
2.9
通讯作者：
Mammi, S
中科院分区：
文献类型：
--
作者：
Bisaglia, M;Schievano, E;Mammi, S
α-突触核蛋白是一种丰富的蛋白质，存在于大脑的突触前终末。该序列的N-端区含有一个不完全的11个残基的周期性，在A类脱脂蛋白中也存在，并能够折叠成两亲性螺旋。在这里，描述了蛋白质的三个片段，分别包括一个、两个和所有重复序列，与不同磷脂组成的囊泡结合的能力。结果表明，在选择TAT-GET膜相互作用时，根据它们的脂质组成，这些重复序列是协同作用的。这一推论可能与蛋白质的生理作用有关，目前对此仍知之甚少。(C)2006年威利期刊公司生物聚合物
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