A hirudin-inspired peptide that clamps both binding sites of thrombin.
Also known as: Angiomax · Angiox
Part of the Foundational & therapeutic peptides cluster
Overview
Bivalirudin is a synthetic 20-amino-acid peptide modeled on the leech anticoagulant hirudin. It binds thrombin bivalently, occupying both the catalytic site and the substrate-recognition exosite, and it is an approved anticoagulant used during percutaneous coronary intervention. This page is educational and not medical advice.
Source & context
Biological / chemical source: Synthetic 20-amino-acid analog of hirudin
Primary research or clinical context: Approved anticoagulant for percutaneous coronary intervention
Bivalent binding
One end of bivalirudin blocks thrombin's active site while a linker spans to the anion-binding exosite, giving high specificity. Modeling the design on hirudin makes it a classic case study of translating a natural anticoagulant into a defined synthetic peptide.
Reversible action
Thrombin slowly cleaves the bound peptide, so inhibition is transient and self-limiting, a property valued in procedural anticoagulation. Bivalirudin is frequently taught alongside heparin to contrast direct versus indirect thrombin inhibition.
FAQ about Bivalirudin
What is Bivalirudin?+
Bivalirudin is a synthetic 20-amino-acid peptide modeled on the leech anticoagulant hirudin. It binds thrombin bivalently, occupying both the catalytic site and the substrate-recognition exosite, and it is an approved anticoagulant used during percutaneous coronary intervention. This page is educational and not medical advice.
Is Bivalirudin an approved medicine?+
Bivalirudin: Approved anticoagulant for percutaneous coronary intervention. Always follow licensed medical guidance for approved products.
What is the typical length of Bivalirudin?+
Bivalirudin is commonly described as approximately 20 amino acids (Direct thrombin inhibitor).