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对人胰岛淀粉样多肽的沉降研究未能检测到低分子量寡聚体。

Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers.

作者信息

Vaiana Sara M, Ghirlando Rodolfo, Yau Wai-Ming, Eaton William A, Hofrichter James

出版信息

Biophys J. 2008 Apr 1;94(7):L45-7. doi: 10.1529/biophysj.107.125146. Epub 2008 Jan 25.

DOI:10.1529/biophysj.107.125146
PMID:18223003
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2267115/
Abstract

Sedimentation velocity experiments show that only monomers coexist with amyloid fibrils of human islet amyloid-polypeptide. No oligomers containing <100 monomers could be detected, suggesting that the putative toxic oligomers are much larger than those found for the Alzheimer's peptide, Abeta(1-42).

摘要

沉降速度实验表明，只有单体与人类胰岛淀粉样多肽的淀粉样纤维共存。未检测到含有少于100个单体的寡聚体，这表明假定的毒性寡聚体比在阿尔茨海默病肽β-淀粉样蛋白（1-42）中发现的那些要大得多。

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本文引用的文献

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Conformation-dependent anti-amyloid oligomer antibodies.构象依赖性抗淀粉样寡聚体抗体。
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The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells.人胰岛淀粉样多肽的聚集潜能决定了其对胰岛β细胞的细胞毒性。
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