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Updated: Jul 13, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
Published on: September 13, 2014
Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement
Montserrat Andújar-Sánchez1, Vicente Jara-Pérez, Ana Cámara-Artigas
1Dpto. 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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