| Abstract
| - Quantitative structure−activity relationship (QSAR) modeling using simple amino acid descriptorswas done on a set of prolyl oligopeptidase (POP) inhibitory peptides derived from β-casein. Usingpartial least-squares regression, a QSAR model was obtained indicating that increased hydrophobicityand molecular bulkiness of amino acids in positions P3, P2, and P1‘ of inhibitory sites on peptidesresulted in increased inhibition (lower IC50). Proline residues were always assumed to be in positionP1. Hydrophobicity and molecular bulkiness have also in other studies been found as important factorsfor binding between substrates (or inhibitors) and the active site of POP. Prolyl oligopeptidase inblood serum is found to influence the level of hormone and neuropeptides and be related to cognitiveand neurological deficiencies, e.g., Alzheimer's disease. Increased knowledge of the relationshipbetween peptides derived from food proteins and their POP inhibition may be important in thedevelopment of functional foods as a supplement to pharmaceutical agents. Keywords: Milk; casein; prolyl oligopeptidase; PEP; POP
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