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Thermodynamic determination of the binding constants of angiotensin‐converting enzyme inhibitors by a displacement method
Author(s) -
Andújar-Sánchez Montserrat,
Jara-Pérez Vicente,
Cámara-Artigas Ana
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.06.048
Subject(s) - enalaprilat , lisinopril , chemistry , isothermal titration calorimetry , captopril , angiotensin converting enzyme , enzyme , binding constant , enalapril , thermodynamics , binding site , biochemistry , blood pressure , endocrinology , biology , physics
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.