Original Research
Funksionele beskrywing van ’n faktor VIIa inhiberende peptied, IP-7, geselekteer deur faagblootleggingstegnologie
Submitted: 22 September 2006 | Published: 22 September 2006
About the author(s)
S.M. Meiring, Departement Hematologie en Selbiologie, Fakulteit Gesondheidswetenskappe, Universiteit van die Vrystaat, Posbus 339 (G2), Bloemfontein, 9300, South AfricaC.E. Roets, Departement Hematologie en Selbiologie, Fakulteit Gesondheidswetenskappe, Universiteit van die Vrystaat, Posbus 339 (G2), Bloemfontein, 9300, South Africa
P.N. Badenhorst, Departement Hematologie en Selbiologie, Fakulteit Gesondheidswetenskappe, Universiteit van die Vrystaat, Posbus 339 (G2), Bloemfontein, 9300, South Africa
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Abstract
Functional characterisation of a factor VIIa inhibiting peptide, IP-7 selected by phage display technology
By using the technique of phage display, we selected a cyclic heptapeptide sequence Cys-Ala-Trp-Pro-His-Thr-Pro-Asp-Cys (C-AWPHTPD-C) that competes with tissue factor for binding to coagulation factor VII. This peptide prolongs the prothrombin time (PT) in a concentration dependent way. It also reduces platelet adhesion to both human endothelial cell and tissue factor matrixes in a flow chamber under arterial flow conditions. Furthermore, it acts as a full competitive inhibitor of factor VIIa with an inhibition constant (Ki) of 123,2 μM. In its current form the peptide is probably not sufficiently potent for development as an antithrombotic agent, but different strategies could be followed to reinforce its performance.
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