FEBS Letters 2007-07-24

Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method.

Montserrat Andújar-Sánchez, Vicente Jara-Pérez, Ana Cámara-Artigas

Index: FEBS Lett. 581(18) , 3449-54, (2007)

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Abstract

Somatic angiotensin I-converting enzyme (s-ACE) plays a central role in blood pressure regulation and has been the target of most antihypertensive drugs. A displacement isothermal titration calorimetry method has been used to accurately determine the binding constant of three strong s-ACE inhibitors. Under the experimental conditions studied in this work, the relative potency of the inhibitors was determined to be enalaprilat>lisinopril>captopril. We analyze the thermodynamic behaviour of the binding process using the new structural information provided by the ACE structures, as well as the conformational changes that occur upon binding.

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