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  • Title: Synthesis of an insulin analogue embodying a strongly fluorescent moiety, [19-tryptophan-A]insulin.
    Author: Ohta N, Burke GT, Katsoyannis PG.
    Journal: J Protein Chem; 1988 Feb; 7(1):55-65. PubMed ID: 3076448.
    Abstract:
    As part of our aim to study the conformation of insulin in solution by time-resolved fluorescence spectroscopy, we have synthesized the analogue [19-Tryptophan-A]insulin. In this compound, the tyrosine residue at position 19 of the A-chain of insulin, one of the most strongly conserved residues in insulins from various species, is substituted with the strongly fluorescent tryptophan residue. [19-Tryptophan-A]insulin displays 4.1 +/- 1.9% of the potency of natural insulin in binding to the insulin receptor from rat liver plasma membranes, 5.0 +/- 2.3% in stimulating lipogenesis in rat adipocytes, and 75.7 +/- 4% of the potency of insulin in radioimmunoassay. In connection with our previous work, these data indicate that an aromatic side chain at position A19 of insulin seems necessary but not sufficient for high biological activity. We further conclude that in regard to the immunogenic determinants of insulin, tryptophan in position A19 is an essentially neutral substitution for tyrosine in that position, in sharp contrast to the situation with regard to biological activity.
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