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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Design and evaluation of nonpeptide fibrinogen gamma-chain based GPIIb/IIIa antagonists.

Two series of nonpeptide turn mimetics were designed by analysis of the solution NMR structure of the 385-411 sequence of the gamma-chain of fibrinogen. These compounds, based on the KQAGD (Lys-Gln-Ala-Gly-Asp, 406-410) sequence, were synthesized and studied in vitro. The most interesting compound from our study, RWJ 50042 (25), exhibits potent inhibition of fibrinogen binding to GPIIb/IIIa (IC50 = 0.009 microM), as well as thrombin- or collagen-induced platelet aggregation (IC50 = 0.76, 0.14 microM). Since the 400-411 sequence is required for gamma-chain bioactivity and is a unique recognition sequence among ligands for integrins, vis-a-vis other RGD (Arg-Gly-Asp)-presenting proteins, these turn mimetics may represent a new, selective approach to antagonism of the fibrinogen receptor.[1]

References

  1. Design and evaluation of nonpeptide fibrinogen gamma-chain based GPIIb/IIIa antagonists. Hoekstra, W.J., Beavers, M.P., Andrade-Gordon, P., Evangelisto, M.F., Keane, P.M., Press, J.B., Tomko, K.A., Fan, F., Kloczewiak, M., Mayo, K.H. J. Med. Chem. (1995) [Pubmed]
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