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  • Title: Inhibition of platelet aggregation of a mutant proinsulin chimera engineered by introduction of a native Lys-Gly-Asp-containing sequence.
    Author: Jing J, Lu S.
    Journal: Biotechnol Lett; 2005 Sep; 27(17):1259-65. PubMed ID: 16215822.
    Abstract:
    An eight amino acid sequence, CAKGDWNC, from disintegrin barbourin, was introduced into an inactive human proinsulin molecule between the B28 and A2 sites to construct a chimeric, anti-thrombosis recombinant protein. The constructed Lys-Gly-Asp (KGD)-proinsulin gene was expressed in Escherichia coli and then purified. The KGD-proinsulin chimera protein inhibits human platelet aggregation, induced by ADP, with an IC50 value (molar concentration causing 50% inhibition of platelet aggregation) of 830 nM: and demonstrates also specific affinity to glycoprotein IIb/IIIa receptor. Its insulin receptor binding activity remains as low as 0.04% with native insulin as a control.
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