desArg9bradykinin

DesArg9-bradykinin, sometimes written des-Arg9-bradykinin, is a peptide fragment derived from bradykinin by enzymatic removal of the C-terminal arginine. The resulting eight-amino-acid peptide is also referred to as bradykinin (1-8). It acts as a selective agonist of the bradykinin B1 receptor, a G protein–coupled receptor that is typically low in healthy tissue but upregulated in inflammation and tissue injury. In contrast, bradykinin itself preferentially activates the B2 receptor.

DesArg9-bradykinin is generated from bradykinin through the action of carboxypeptidases, particularly kininase I enzymes such as carboxypeptidase N, during inflammatory states. It is rapidly inactivated by peptidases in the circulation and tissues, contributing to its short-lived action.

Physiological and pathophysiological roles include mediation of pain, edema, and vascular permeability in inflamed or injured tissues via B1 receptor signaling. The desArg9‑BK–B1 axis is thought to contribute to chronic inflammatory processes and may participate in conditions such as inflammatory pain and some forms of angioedema, especially where B1 receptor expression is elevated.

In research, desArg9-bradykinin serves as a selective B1 receptor agonist and is used to study B1 receptor–mediated signaling. Pharmacological modulation of the B1 receptor remains a potential strategy for inflammatory disorders, though clinical applications are still under investigation.