In vitro inhibitor effect and molecular docking of thiamine (vitamin B 1 ), riboflavin (vitamin B 2 ), and reference inhibitor captopril on angiotensin-converting enzyme purified from sheep plasma.

Autor: Ciftci MH; Science Faculty, Chemistry Department, Van Yüzüncü Yıl University, Van, Turkey., Turkoglu V; Science Faculty, Chemistry Department, Van Yüzüncü Yıl University, Van, Turkey., Bas Z; Health Sciences Faculty, Nutrition and Dietetics Department, Van Yüzüncü Yıl University, Van, Turkey., Celikezen FC; Science and Letter Faculty, Department of Chemistry, Bitlis Eren University, Bitlis, Turkey.
Jazyk: angličtina
Zdroj: Archives of physiology and biochemistry [Arch Physiol Biochem] 2024 Dec; Vol. 130 (6), pp. 974-983. Date of Electronic Publication: 2024 Jul 10.
DOI: 10.1080/13813455.2024.2376814
Abstrakt: Objective: Angiotensin-converting enzyme (ACE, EC 3.4.15.1) is a very important factor in the regulation of blood pressure. Also, the inhibition of ACE with natural compounds has been a very important research area in the treatment of high blood pressure. ACE was purified and characterized from sheep plasma. Molecular docking studies and the inhibition effect of thiamine, riboflavin, and captopril on ACE were investigated.
Methods: Herein, ACE was purified from sheep plasma by affinity chromatography. The effect of thiamine and riboflavin on ACE was researched. Molecular docking studies were performed to understand the molecular interactions between thiamine, riboflavin, and captopril with ACE.
Results: The purification coefficient was found to be 8636 fold. The binding energy of thiamine, riboflavin, and captopril was found to be -6.7 kcal/mol, -8.1 kcal/mol, and -5.5 kcal/mol, respectively. Thiamine conformed to three conventional hydrogen bonds with ASP:415, HIS:513, and LYS:454. Riboflavin formed four conventional hydrogen bonds with GLN:281, GLU:376, THR:282, and TYR:520. Captopril formed two conventional hydrogen bonds with ARG:124, one conventional hydrogen bond with TYR:62 and ASN:85, and one carbon-hydrogen bond with ASN:66. Molecular docking results showed that thiamine, riboflavin, and captopril interacted with ACE through hydrogen bonding and hydrophobic interactions. Thiamine and riboflavin indicated significant inhibition effects on ACE. The IC 50 values of thiamine, riboflavin, and captopril were found as 960.56 µM, 11.02 µM, and 1.60 nM, respectively. K i values for thiamine, riboflavin, and captopril were determined as 1352.04 µM, 12.30 µM, and 1.06 nM, respectively.
Conclusion: In this work, it was concluded that thiamine and riboflavin may have preventive and therapeutical impacts against high blood pressure with their ACE inhibitor effect. Thiamine and riboflavin showed a lower inhibitory effect with a higher IC 50 than captopril. However, when the inhibitory effect of thiamine and riboflavin vitamins is compared to captopril, it is concluded that they may be natural inhibitors with fewer side effects.
Databáze: MEDLINE
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