Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method.
Article Details
- CitationCopy to clipboard
Andujar-Sanchez M, Jara-Perez V, Camara-Artigas A
Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method.
FEBS Lett. 2007 Jul 24;581(18):3449-54. Epub 2007 Jun 27.
- PubMed ID
- 17618628 [ View in PubMed]
- 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.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Captopril Angiotensin-converting enzyme Protein Humans YesInhibitorDetails Enalapril Angiotensin-converting enzyme Protein Humans YesInhibitorDetails Lisinopril Angiotensin-converting enzyme Protein Humans YesInhibitorDetails