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How α-Crystallin Prevents the Aggregation of Insulin

机译:α-晶体蛋白如何预防胰岛素的聚集

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摘要

Using steady-state, polarized, and phase-modulation fluorometry, the dithiothreitol-induced denaturation of insulin and formation of its complex with α-crystallin in solution were studied. Prevention of the aggregation of insulin by α-crystallin is due to formation of chaperone complexes, i.e. interaction of chains of the denatured insulin with α-crystallin. The conformational changes in α-crystallin that occur during complex formation are rather smaE. It is unlikely that N-ter-mini are directly involved in the complex formation. The 8-anilino-1-naphthalenesulfonate (ANS) is not sensitive to the complex formation. ANS emits mainly from α-crystallin monomers, dimers, and tetramers, but not from oligomers or aggregates. The possibility of highly sensitive detection of aggregates by light scattering using a spectrofluorometer with crossed monochromators is demonstrated.
机译:使用稳态,偏振和相位调制荧光法,研究了二硫苏糖醇诱导的胰岛素变性以及其与α-结晶蛋白在溶液中的复合物的形成。 α-晶状体蛋白防止胰岛素聚集是由于分子伴侣复合物的形成,即变性的胰岛素链与α-晶状体蛋白的相互作用。在复合物形成过程中发生的α-晶体蛋白构象变化相当大。 N-ter-mini不可能直接参与复合物的形成。 8-苯胺基-1-萘磺酸盐(ANS)对复合物的形成不敏感。 ANS主要从α-晶状蛋白单体,二聚体和四聚体发出,但不从低聚物或聚集体发出。证明了使用带有交叉单色仪的荧光分光光度计通过光散射高灵敏度检测聚集体的可能性。

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