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

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

  • FEBS Lett. 2007 Jul 24;581(18):3449-54. doi: 10.1016/j.febslet.2007.06.048.
Montserrat Andújar-Sánchez 1 Vicente Jara-Pérez Ana Cámara-Artigas
Affiliations

Affiliation

  • 1 Dpto. Química Física, Bioquímica y Química Inorgánica, Universidad de Almería, Carretera Sacramento s/n, Almería 04120, Spain.
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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