Aspartame and aspartame derivatives effect human thrombin catalytic activity
Copyright policy )Aspartame and aspartame derivatives effect human thrombin catalytic activity
The study of small Asp-Phe analogs was undertaken since this dipeptide sequence is critical in fibrinogen recognition and catalysis. The inhibition of clotting activity by Asp-Phe-methyl ester (aspartame), formyl-Asp-Phe-methyl ester and acetyl-Asp-Phe was biphasic in all cases, indicating the presence of at least two binding sites. The N-terminally blocked derivatives are stronger inhibitors than aspartame. In contrast, tosyl-Gly-Pro-Arg-p'-nitroanilide hydrolysis was inhibited minimally by Asp-Phe-methyl, ester [Ki(app)=98 mM]. Acetyl-Asp-Phe inhibition of thrombin amidase activity was biphasic, tenfold stronger and appeared to be strongly cooperative. These results are discussed with respect to the inhibition of alpha-thrombin by ATP.
- University of Denver United States
Binding Sites, Thrombin, Humans, Amino Acid Sequence, Dipeptides, Aspartame, Blood Coagulation, Catalysis, Amidohydrolases
Binding Sites, Thrombin, Humans, Amino Acid Sequence, Dipeptides, Aspartame, Blood Coagulation, Catalysis, Amidohydrolases
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