Changes of conformation and aggregation state induced by binding of lanthanide ions to insulin |
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Authors: | Yi?Cheng Rongchang?Li Email author" target="_blank">Kui?WangEmail author |
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Institution: | 1. Department of Chemical Biology, School of Pharmaceutical Sciences, Peking University, Beijing 100083, China;Present address: Department of Cell Biology and Physiology, University of Pittsburgh, Pittsburgh, PA 15261, USA 2. Department of Chemical Biology, School of Pharmaceutical Sciences, Peking University, Beijing 100083, China |
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Abstract: | To clarify the mechanism of lanthanide ions (Ln3+) on the across-membrane transport of insulin and subsequent reducing blood glucose, the interactions of Ln3+with Zn-insulin and Zn-free insulin are investigated by spectroscopic methods. The results reveal that the binding of Ln3+ to insulin can induce its structure changes from secondary to quaternary structure, depending on the Ln3+ concentration. In the lower concentration, it triggers the conformational changes of insulin monomer in the binding region with insulin receptor (B(24-30)). It would affect insulin-insulin receptor interaction. Moreover, Ln3+ binding promotes the assembly of insulin monomer from dimer to polymer. The potency of Ln3+ in inducing insulin's aggregation is stronger than that of Zn2+. Furthermore, the aggregation can be reversed partly by EDTA-treatment, indicating that it is not due to denaturation. Similar to Zn2+ effect, Ln3+ can stabilize insulin hexamer in a certain range of concentration, but is stronger than the former. |
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Keywords: | insulin lanthanide conformation aggregation |
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