Abstract

Angiotensin converting enzyme (ACE) catalyses the conversion of angiotensin I to angiotensin II a potent vasoconstrictor in a substrate concentration dependent manner and degrades bradykinin a potent vasodilator and other vasoactive peptides which leads to increase in blood pressure. Prolonged increase in blood pressure condition increases the risk of heart attacks, heart failure, stroke, or kidney failure. Naturally occurring when proteins acts as angiotensin converting enzyme inhibitor. Inhibition of angiotensin converting enzyme by angiotensin converting enzyme inhibitors results in the decreased formation of angiotensin II and decreased metabolism of bradykinin leading to systematic dilation of the arteries and veins and a decrease in arterial blood pressure. The molecular docking analysis done indicates that the receptor of human angiotensin converts enzyme through an interaction with the chemical bonds and the bovine ligand whey proteins - beta-lactoglobulin, alpha-lactalbumin, serum albumin and immunoglobulins effectively. The bovine ligand whey proteins - beta-lactoglobulin, alpha-lactalbumin, serum albumin and immunoglobulins are safer and milder with fewer or no side effects than the drugs currently used in the treatment of lessening high blood pressure which can be better used for the development of new therapeutics to decrease formation of angiotensin II and to decrease inactivation of bradykinin as a means of inhibiting angiotensin converting enzyme lessening high blood pressure there by reducing the risk factors of heart attacks, heart failure, stroke, or kidney failure.

Key words: Angiotensin converting enzyme, whey proteins, beta-lactoglobulin, alpha-lactalbumin, serum albumin, immunoglobulins, hex, molecular docking, intermolecular bonding interactions, high blood pressure.