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

Authors
  • Andújar-Sánchez, Montserrat
  • Jara-Pérez, Vicente
  • Cámara-Artigas, Ana
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Jul 24, 2007
Volume
581
Issue
18
Pages
3449–3454
Identifiers
PMID: 17618628
Source
Medline
License
Unknown

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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