FEBS Lett. 2007 Jul 24;581(18):3449-54. Epub 2007 Jun 27.

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

Andújar-Sánchez M, Jara-Pérez V, Cámara-Artigas A.

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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.

PMID:: 17618628; [PubMed - indexed for MEDLINE]

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