Abstract
We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51- found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin. The compound is indistinguishable from a previously reported compound whose A-chain corresponds to the A- and D-domains of IGF-I without the substitution, in assays for insulin-like activity as well as in assays for growth-promoting activity. We conclude that these A-domain residues do not contribute significantly to the interaction of IGF-I with either insulin or IGF-I receptors.
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A preliminary discussion of this work was presented (P.G.K.) to the 19th European Peptide Symposium, Porto Carras, Greece, 1986.
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Joshi, S., Burke, G.T. & Katsoyannis, P.G. An insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to a modified A- and the D-domains of human insulin-like growth factor I. J Protein Chem 9, 235–246 (1990). https://doi.org/10.1007/BF01025314
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DOI: https://doi.org/10.1007/BF01025314