There are many causes of hypertension; angiotensin converting enzyme (ACE) is wellidentified for its important physiological roles in the regulation of blood pressure. ACE converts angiotensin-I, an inactivedecapeptide, to angiotensin-II, a potent vasoconstrictoroctapeptide [1].Nowadays, peptides have been found to possess many physiological functions such as antioxidant, antimicrobial, antithrombotic and antihypertensiveactivities [2]. The objective of the present study was to insilico analysis of the ACE-inhibitory activity of TR-14 peptide obtained from ostrich serum hydrolysate. The interaction between TR-14 peptide and N- domain (4APJ)as well as C- domain (3L3N ) of ACE was stimulated using MVD software.The chemical structure of TR-14 was constructed by MOE software. Furthermore, Energy minimization of peptide was performed by GizMOE minimizer method.ACE domainswere tested by means of different softwaressuch as PROCHECK and ERRAT [3].Following simulation process, the best configuration of TR-14 binding into N and C domains of ACE was selected and the results (table 1) used for further analysis. Our results demonstrated that the inhibiting constant of TR-14 - N-domain complexwas very smaller than that of the TR-14 - C-domain complex.Therefore, TR-14 peptide has more affinity binding to C-domain with Moldockscore of -104.483. In conclusion, the results of docking simulation can help us in the interpretation ofin vitro results

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