The 4th International Conference on Nursing

Author :

Shila Wisnasari

Affiliation :

School of Nursing, Universitas Brawijaya, Malang, Indonesia

Abstract :

Introduction ACE gene polymorphism is thought responsible to the different response to ACE inhibitor therapy in hypertensive patients. Angiotensin I-converting enzyme (ACE) has two homologous catalytic domains, the N- and C-domains. Alu insertion (I allele) in the intron 16 of ACE resulted in premature codon termination so the I variant has only one active site in the N-domain while the Alu deletion (D variant) still has two active sites of ACE. The inhibitory potency of ACE inhibitors such as lisinopril and captopril on Hypertensive Patients with ACE I/D Polymorphism, mainly determined by differences in the binding affinity, is still not widely known. This study was conducted to investigate the inhibitory potency of lisinopril and captopril by analyzing the binding affinity of ACE protein (I and D variant) to lisinopril and captopril in silico. Methods Binding affinity of lisinopril and captopril with ACE protein (I and D variant) was obtained from molecular docking using AutodockVina. Results Docking calculation showed lisinopril has the higher binding affinity to the C-domain (-8.8 kcal/mol) than N-domain ACE (-7.3 kcal/mol), means that lisinopril was found to be more effective to inhibit D variant of ACE protein activity. Captopril showed the same binding affinity of captopril in both N- and C-domain (-6.1 kcal/mol). This result implied that captopril showed the same inhibitory activity towards I and D variant of ACE. Conclusion Lisinopril and captopril apparently showed different inhibitory potency between I and D variant of ACE, as proven by calculated binding affinity.

Keywords :

ACE; Binding Affinity; Lisinopril; Captopril