35 MHz quartz crystal microbalance and surface plasmon resonance studies on the binding of angiotensin converting enzyme with lisinopril.
Angiotensin converting enzyme (ACE) plays a pivotal role in blood pressure regulation, and its interaction with an ACE inhibitor (ACEI) is an important research topic for treatment of hypertension. Herein, a low reagent consumption, multiparameter and highly sensitive quartz crystal microbalance (QCM) at 35-MHz fundamental frequency was utilized to monitor in situ the binding process of solution lisinopril (LIS, a carboxylic third-generation ACEI) to ACE adsorbed at a 1-dodecanethiol (C12SH)-modified Au electrode. From the QCM data, the binding molar ratio (r) of LIS to adsorbed ACE was estimated to be 2.3:1, and the binding and dissociation rate constants (k(1) and k(-1)) and the binding equilibrium constant (K(a)) were estimated to be k(1)=4.1×10(6) L mol(-1) s(-1), k(-1)=7.3×10(-3) s(-1) and K(a)=5.62×10(8) L mol(-1), respectively. Comparable qualitative and quantitative results were also obtained from separate experiments of cyclic voltammetry, electrochemical impedance spectroscopy and surface plasmon resonance measurements.
Key Laboratory of Chemical Biology and Traditional Chinese Medicine Research (Ministry of Education of China), College of Chemistry and Chemical Engineering, Hunan Normal University, Changsha, PR China.
Zhaohong
Z
Su
Li
L
Chen
Ying
Y
Liu
Xiuhui
X
He
Yaping
Y
Zhou
Qingji
Q
Xie
Shouzhuo
S
Yao
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000494:pharmacology*; D000959:Antihypertensive Agents / Q000494:pharmacology*; D006801:Humans; D017706:Lisinopril / Q000494:pharmacology*; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D011485:Protein Binding; D058525:Quartz Crystal Microbalance Techniques / Q000379:methods*; D020349:Surface Plasmon Resonance / Q000379:methods*
D000806:Angiotensin-Converting Enzyme Inhibitors; D000959:Antihypertensive Agents; D017706:Lisinopril; D007703:Peptidyl-Dipeptidase A