Roles of Antifibrinolytics in Cosmetics and the Absence of Aprotinin Additives as a Consumer-Bought Anti-Aging Agent

https://doi.org/10.65161/rec7oAvvrmXEAEquX

Plasmin is a “skin aging” enzyme that contributes to the production of wrinkles and inflammation, which is produced from plasminogen. This study examines the roles of antifibrinolytics in inhibiting plasminogen through the medium of cosmetic products, primarily dominated by tranexamic acid (TXA) and epsilon-aminocaproic acid (EACA), as established antifibrinolytic agents. Because aprotinin is a powerful antifibrinolytic agent not found in cosmetic products, a disparity was observed. To resolve this, the mechanisms and properties of each antifibrinolytic were analyzed. TXA and EACA were found to be lysine analogs, and aprotinin is a bovine polypeptide derived from lung tissue that serves as a serine-protease inhibitor. Because aprotinin is banned in the United States, is difficult to isolate, and has too large a molecular weight to penetrate the skin, it was found that aprotinin is unlikely to function for “anti-aging” properties on the epidermis.