A peptide with hypocholesterolemic activity was isolated by HPLC from the pepsin hydrolysate of 11S-globulin. Its molecular weight (755.2 Da) and amino-acid sequence (Ile-Ala-Val-Pro-Gly-Glu-Val-Ala) were established. The hypocholesterolemic effect was determined by analysis of bile-acid binding and the percent inhibition of 3-hydroxy-3-methylglutaryl coenzyme A reductase in vitro. The lowering of the cholesterol content is explained by bile acids bound to hydrolysate peptides shielding them from reabsorption and stimulating the transformation of cholesterol in blood plasma.

was analyzed using results from a semi-empirical PM3 method. The similarity of the peptide structures to NADPH was determined by comparing the relative contribution from projections of selected bond lengths in the peptides in two mutually perpendicular planes to the corresponding bond lengths in the nicotinamide part of the substrate. The correlation coefficient between the calculated average values of the relative contributions of the bonds and the inhibitory activity of these peptides is rather high (R = 0.926). This indicates that these peptides can occupy the part of the binding site for NADPH in the active center of the enzyme.

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