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Amyloid fibril formation and chaperone-like activity of peptides from alpha A-Crystallin

机译：淀粉样蛋白原纤维形成和α-晶体蛋白肽的伴侣样活性

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alpha A-Crystallin (alpha AC), a major component of eye lens, exhibits chaperone-like activity and is responsible for maintaining eye lens transparency. Synthetic peptides which corresponded to the putative substrate-binding site of alpha AC have been reported to prevent aggregation of proteins [Sharma, K. K., et al. (2000) J. Biol. Chem. 275, 3767-3771]. In this study, we found that these peptides, alpha AC(70-88), the peptide corresponding to amino acids 70-88 of alpha AC (KFVIFLDVKHFSPEDLTVK), and alpha AC(71-88), suppressed the amyloid fibril formation of amyloid beta protein (A beta). On the other hand, while alpha AC(71-88) exhibited chaperone-like activity toward insulin, alpha AC(70-88) and alpha AC(70-88)K70D promoted rapid growth of aggregates consisting of insulin and these peptides in their solution mixtures. Interestingly, we found that alpha AC(71-88) itself can also form amyloid fibrils. It is possible that the chaperone-like activity of the alpha AC peptides is potentially related to their propensity for amyloid fibril formation. Analysis of variants of the alpha AC peptides suggested that F71 is important for amyloid formation, and interestingly, this same residue has previously been found to be essential for chaperone-like activity. Amyloid fibril formation was also observed with the shorter peptide, alpha AC(70-76)K70D, showing that the ability to form amyloid fibrils is maintained even with significant deletion of the C-terminal sequence. The formation of amyloid fibril was suppressed in alpha AC(70-88), suggesting that the K70 in the substrate binding site may play a role in suppressing the amyloid fibril formation of alpha AC, which agreed with recent proposals about the presence of an aggregation suppressor in the region flanking aggregation-prone hydrophobic sequences.
机译：晶状体的主要成分-α-晶状体蛋白（αAC）表现出类似伴侣的活性，并负责保持晶状体的透明性。据报道，对应于αAC假定的底物结合位点的合成肽可防止蛋白质聚集[Sharma，K.K。，等人。 （2000）生物化学杂志。化学275，3767-3771]。在这项研究中，我们发现这些肽αAC（70-88），与αAC（KFVIFLDVKHFSPEDLTVK）的氨基酸70-88相对应的肽和αAC（71-88）抑制了淀粉样蛋白的淀粉样蛋白原纤维形成。 beta蛋白（A beta）。另一方面，尽管αAC（71-88）对胰岛素表现出类似伴侣的活性，但是αAC（70-88）和αAC（70-88）K70D促进了由胰岛素及其肽组成的聚集体的快速生长。溶液混合物。有趣的是，我们发现αAC（71-88）本身也可以形成淀粉样原纤维。 αAC肽的伴侣样活性可能与它们形成淀粉样蛋白原纤维的倾向有关。对αAC肽变体的分析表明，F71对于淀粉样蛋白的形成很重要，有趣的是，以前已经发现该相同残基对于分子伴侣样活性是必不可少的。还用较短的肽αAC（70-76）K70D观察到淀粉样蛋白原纤维的形成，表明即使显着缺失C端序列，淀粉样蛋白原纤维的形成能力也得以保持。淀粉样蛋白原纤维的形成在αAC（70-88）中被抑制，这表明底物结合位点中的K70可能在抑制αAC的淀粉样原纤维形成中起作用，这与关于聚集存在的最新提议相一致。在易于聚集的疏水序列侧翼的区域中存在抑制子。

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