The thermodynamic stability of insulin disulfides is not affected by the C-domain of insulin-like growth factor 1 |
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Authors: | Guo Zhanyun and Feng Youmin |
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Institution: | State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China |
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Abstract: | Both Insulin and insulin-like growth factor 1 are members of insulin superfamily. They share homologous primary and tertiary
structure as well as weakly overlapping biological activity. However, their folding behavior is different: insulin and its
recombinant precursor (PIP) fold into one unique tertiary structure, while IGF-1 folds into two disulfides isomers with similar
thermodynamic stability. To elucidate the molecular mechanism of their different folding behavior, we prepared a singlechain
hybrid of insulin and IGF-1, B10Glu]Ins/IGF-1(C), and studied its folding behavior compared with that of PIP and IGF-1. We
also separated a major non-native disulfides isomer of the hybrid and studied its refolding. The data showed that the C-domain
of IGF-1 did not affect the folding thermodynamics of insulin, that is, the primary structure of the hybrid encoded only one
thermodynamically stable disulfides linkage. However, the folding kinetics of insulin was affected by the C-domain of IGF-1. |
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Keywords: | insulin insulin-like growth factor 1 hybrid unfolding refolding |
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