An insulin-like hybrid consisting of a modified A-domain of human insulin-like growth factor I and the B-chain of insulin |
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| Authors: | Lin Zong G. Thompson Burke Panayotis G. Katsoyannis |
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| Affiliation: | (1) Department of Biochemistry, Mount Sinai School of Medicine of the City University of New York, New York, New York;(2) Department of Biochemistry, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1020, 10029-6574 New York, New York |
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| Abstract: | We have synthesized an insulin-like compound, consisting of the B-chain of bovine insulin and an A-chain corresponding to the A-domain of human insulin-like growth factor-I (IGF-I), in which the isoleucine residue normally present in position 2 of the A-domain of IGF-I has been replaced with glycine. Biological evaluation of the compound indicated that its insulin-like activity (insulin receptor-binding and stimulation of lipogenesis) was 0.2%, and its growth-factor activity (stimulation of thymidine incorporation) was less than 1%, both relative to natural insulin. We conclude that interactions between IleA2 and TyrA19, which are crucial to high biological activity in insulin, are also present in IGF-I, and are equally critical for its biological activity. |
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| Keywords: | IGF-I/insulin hybrid growth-promoting activity insulin activity structure-function relationships |
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