The presented work allows one to speculate that the hydrophobic contacts of the residues
located at the P2 and P3 positions with the corresponding subsites of thrombin (S2
and S3) allow the synthesis of compounds that can react with thrombin specifically
and probably may not interact with other trypsin-like serine proteases. Substitution
of proline by m-Abz-residue may result in the development of novel substrates and
inhibitors for thrombin.
Thrombin - antithrombin - D-Phe-Pro-Gly-amide - arginine - enzyme inhibition
