Inhibition of Platelet Aggregation of a Mutant Proinsulin Chimera Engineered by Introduction of a Native Lys-Gly-Asp-containing Sequence |
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Authors: | Email author" target="_blank">Jian?JingEmail author Shan?Lu |
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Institution: | (1) Department of Biochemistry and Biotechnology, Laboratory of Biotechnology and Protein Engineering, Beijing Normal University, 100875 Beijing, China |
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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 remaines
as low as 0.04% with native insulin as a control. |
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Keywords: | glycoprotein IIb/IIIa receptor inhibition of platelet aggregation KGD (Lys-Gly-Asp) motif proinsulin mutant |
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