TAILIEUCHUNG - Báo cáo khoa học: Insulin is a kinetic but not a thermodynamic inhibitor of amylin aggregation

One of the most important pathological features of type 2 diabetes is the formation of islet amyloid, of which the major component is amylin pep-tide. However, the presence of a natural inhibitor such as insulin may keep amylin stable and physiologically functional in healthy individuals. Some previous studies demonstrated that insulin was a potent inhibitor of amylin fibril formationin vitro, but others obtained contradictory results. | ỊFEBS Journal Insulin is a kinetic but not a thermodynamic inhibitor of amylin aggregation Wei Cui Jing-wen Ma Peng Lei Wei-hui Wu Ye-ping Yu Yu Xiang Ai-jun Tong Yu-fen Zhao and Yan-mei Li Department of Chemistry Key Laboratory of Bioorganic Phosphorus Chemistry and ChemicalBiology Ministry of Education Tsinghua University Beijing China Keywords aggregation amylin inhibition insulin type 2 diabetes Correspondence . Li Department of Chemistry Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology Ministry of Education Tsinghua University Beijing 100084 China Fax 86 10 62781695 Tel 86 10 62796197 E-mail liym@ Received 8 January 2009 revised 3 April 2009 accepted 15 April 2009 doi One of the most important pathological features of type 2 diabetes is the formation of islet amyloid of which the major component is amylin peptide. However the presence of a natural inhibitor such as insulin may keep amylin stable and physiologically functional in healthy individuals. Some previous studies demonstrated that insulin was a potent inhibitor of amylin fibril formation in vitro but others obtained contradictory results. Hence it is necessary to elucidate the effects of insulin on amylin aggregation. Here we report that insulin is a kinetic inhibitor of amylin aggregation only keeping its inhibitory effect for a limited time period. Actually insulin promotes amylin aggregation after long-term incubation. Furthermore we found that this promotional effect could be attributed to the copolymerization of insulin and amylin. We also found that insulin copolymerized with amylin monomer or oligomer rather than preformed amylin fibrils. These results suggest that the interaction between insulin and amylin may contribute not only to the inhibition of amylin aggregation but also to the coaggregation of both peptides in type 2 diabetes. Amylin or islet amyloid polypeptide a 37 amino acid peptide is the major component

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