Amyloidogenic synthetic peptides of β2-microglobulin -: a role of the disulfide bond
Amyloidogenic synthetic peptides of β2-microglobulin -: a role of the disulfide bond
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DOI：
10.1016/s0006-291x(03)00543-6
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发表时间：
2003-04-25
影响因子：
3.1
通讯作者：
Naiki, H
中科院分区：
文献类型：
--
作者：
Hasegawa, K;Ohhashi, Y;Naiki, H
为了寻找β 2-微球蛋白（β 2-m）淀粉样蛋白原纤维形成的关键区域，我们合成了6个肽，对应于β 2-m天然结构中7个β折叠中的6个，并检查了它们的淀粉样蛋白原性。在检测的肽中，肽（21-31）（链13）和肽（21-31）和（78-86）的混合物（链F）在pH 2.5和7.5下均显示原纤维形成。肽（21-31）是先前报道的β 2-m的蛋白水解片段Ser 21-Lys 41（K3）的N-末端的一半，表明该区域可能是必需的核心。有趣的是，通过二硫键形成的肽（21-31）的二聚体基本上促进了原纤维的形成，表明二硫键对于原纤维的结构稳定性是重要的。(C)2003 Elsevier Science（美国）。All rights reserved.
To search for the essential regions responsible for the beta2-microglobulin (beta2-m) amyloid fibril formation, we synthesized six peptides corresponding to six of the seven beta-sheets in the native structure of beta2-m, and examined their amyloidogenicity. Among the peptides examined, peptide (21-31) (strand 13) and the mixture of peptide (21-31) and (78-86) (strand F) showed fibril formation at both pH 2.5 and 7.5. Peptide (21-31) is the N-terminal half of the previously reported proteolytic fragment of beta2-m, Ser21-Lys41 (K3), suggesting that this region may be the essential core. Interestingly, the dimer formation of peptide (21-31) by the disulfide bond substantially facilitated the fibril formation, indicating that the disulfide bond is important for the structural stability of the fibrils. (C) 2003 Elsevier Science (USA). All rights reserved.