Novel heparin mimetics reveal cooperativity between exosite 2 and sodium-binding site of thrombin.

ABSTRACT:

Introduction

Thrombin is a primary target of most anticoagulants. Yet, thrombin's dual and opposing role in pro- as well as anti- coagulant processes imposes considerable challenges in discovering finely tuned regulators that maintain homeostasis, rather than disproportionately changing the equilibrium to one side. In this connection, we have been studying exosite 2-mediated allosteric modulation of thrombin activity using synthetic agents called low molecular weight lignins (LMWLs). Although the aromatic scaffold of LMWLs is completely different from the polysaccharidic scaffold of heparin, the presence of multiple negatively charged groups on both ligands induces binding to exosite 2 of thrombin. This work characterizes the nature of interactions between LMWLs and thrombin to und

SUBMITTER: Abdel Aziz MH 

PROVIDER: S-EPMC5943173 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature