Bivalirudin API Powder CAS 128270-60-0

Bivalirudin API Powder is a synthetic 20‑amino‑acid peptide serving as a specific, reversible, bivalent direct thrombin inhibitor. Engineered as a optimized hirudin analog, it simultaneously binds to thrombin’s active catalytic site and anion‑binding exosite I, delivering potent, precise and highly predictable anticoagulant activity for pharmaceutical research and formulation development.

Featuring a unique bivalent binding mechanism, Bivalirudin directly suppresses both free and clot‑bound thrombin independent of antithrombin cofactors, fundamentally differing from conventional heparin‑based anticoagulants. Unlike natural hirudin, its inhibitory effect is fully reversible: thrombin gradually cleaves the internal Arg3‑Pro4 bond of the peptide, steadily restoring thrombin activity. This reversible cleavage mechanism endows Bivalirudin with a short half‑life and controllable pharmacokinetic performance, enabling safer and more predictable anticoagulation outcomes for clinical and preclinical applications.

Derived from natural leech‑sourced hirudin, Bivalirudin consists of a bioactive D‑Phe‑Pro‑Arg‑Pro N‑terminal tetrapeptide linked to a C‑terminal dodecapeptide via a tetraglycine spacer. It is a mature, pharmacopoeia‑grade peptide API widely adopted for parenteral anticoagulant formulation research and production. 

1. Study of bivalent thrombin binding and reversible anticoagulant pathways

2. Functional comparison between direct thrombin inhibitors and heparin‑based anticoagulants

3. Core API intermediate for injectable anticoagulant formulation development

4. Preclinical modeling of controllable short‑term anticoagulation therapy

5. Functional research on hirudin analog modification and linker design