Abstract
Thrombin is a critical serine protease in the coagulation system and is widely used as a target protein for antithrombotics. Spectroscopic analysis is a simple and effective method that is used to study the interaction between small molecules and proteins. In this study, the interactions of a potential antithrombotic peptide AGFAGDDAPR (P10) with thrombin were investigated by fluorescence spectroscopy, UV-vis spectroscopy, circular dichroism, Fourier-transform infrared spectroscopy and Raman spectroscopy, respectively. The results showed that the peptide P10 bonded to thrombin via hydrogen bonding and van der Waals forces, resulting in fluorescence quenching. And, the secondary structure of thrombin changed, the β-sheet decreased, and the random coil increased. The peptide P10 bonded to proline and lysine, and changed the space structure of thrombin, resulting in inhibition of thrombin activity. The results contributed to exploration of the mechanism of this potential antithrombotic drug interaction with thrombin in order to provide a preliminary understanding of the pharmacodynamic properties of P10.