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首页> 外文期刊>Biochemistry >Anti-Amyloid Activity of the C-Terminal Domain of proSP-C against Amyloid β-Peptide and Medin
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Anti-Amyloid Activity of the C-Terminal Domain of proSP-C against Amyloid β-Peptide and Medin

机译：proSP-C的C末端结构域对淀粉样β肽和Medin的抗淀粉样活性

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摘要

Amyloid fibrils are found in ∼25 different diseases, including Alzheimer’s disease. Lungnsurfactant protein C (SP-C) forms fibrils in association with pulmonary disease. It was recently foundnthat the C-terminal domain of proSP-C (CTC), which is localized to the endoplasmic reticulum (ER)nlumen, protects the transmembrane (TM) part of (pro)SP-C from aggregation into amyloid until it has anfolded into an R-helix. CTC appears to have a more general anti-amyloid effect by also acting on TMnregions of other proteins. Here we investigate interactions of CTC with the amyloid u0001-peptide (Au0001)nassociated with Alzheimer’s disease and medin, a peptide that forms fibrils in the most common form ofnhuman amyloid. CTC prevents fibril formation in Au0001 and medin and forms a complex with Au0001 oligomers,nas judged by size-exclusion chromatography and electrospray ionization mass spectrometry. These datansuggest that CTC functions as a chaperone that acts preferentially against unfolded TM segments andnstructural motifs found during amyloid fibril formation, a mechanism that may be exploited in forming anbasis for future anti-amyloid therapy.
机译：淀粉样蛋白原纤维存在于大约25种不同的疾病中，包括阿尔茨海默氏病。肺表面活性剂蛋白C（SP-C）与肺部疾病形成原纤维。最近发现，proSP-C（CTC）的C末端结构域位于内质网（ER）内腔，可保护（pro）SP-C的跨膜（TM）部分免于聚集成淀粉样蛋白，直至其折成R螺旋。通过对其他蛋白质的TMn区域也起作用，CTC似乎具有更普遍的抗淀粉样蛋白作用。在这里，我们研究了CTC与与阿尔茨海默氏病和麦丁（medin）无关的淀粉样蛋白u0001肽（Au0001）的相互作用，该肽以人类淀粉样蛋白的最常见形式形成原纤维。 CTC可防止原纤维在Au0001和medin中形成，并与Au0001低聚物形成复合物。这些数据表明，CTC可以作为伴侣分子，优先对抗淀粉样蛋白原纤维形成过程中发现的未折叠的TM段和结构性基序，该机制可用于形成无花果，以用于未来的抗淀粉样蛋白治疗。

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