A new direction for anticoagulants: inhibiting fibrin assembly with PEGylated fibrin knob mimics.

ABSTRACT: Current anticoagulants target coagulation factors upstream from fibrin assembly and polymerization (i.e., formation of fibrin clot). While effective, this approach requires constant patient monitoring since pharmacokinetics and pharmacodynamics vary from patient to patient. To address these limitations, we developed an alternative anticoagulant that effectively inhibits fibrin polymerization. Specifically, we investigated PEGylated fibrin knob "A" peptides, evaluating the effect of both polyethylene glycol (PEG) chain length (0, 2, 5, and 10-30 kDa) and knob peptide sequence (GPRPAAC, GPRPFPAC, and GPRPPERC) on inhibiting fibrin polymerization (i.e., clot formation). Thrombin-initiated clotting assays with purified fibrinogen were performed to compare clot formation with each peptide-PEG c

SUBMITTER: Stabenfeldt SE 

PROVIDER: S-EPMC3168719 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature