An ab initio conformational study on captopril

Autor:	Ladislaus L. Torday, Graciela N. Zamarbide, Mario R. Estrada, M.A. Zamora, Francisco Tomás Vert, Imre G. Csizmadia, Ricardo D. Enriz
Rok vydání:	2003
Předmět:	biology Stereochemistry Hydrogen bond Ab initio Active site Captopril Angiotensin-converting enzyme Condensed Matter Physics Biochemistry chemistry.chemical_compound chemistry ACE inhibitor biology.protein medicine Moiety Physical and Theoretical Chemistry Guanidine medicine.drug
Zdroj:	Journal of Molecular Structure: THEOCHEM. :599-608
ISSN:	0166-1280
DOI:	10.1016/j.theochem.2003.08.084
Popis:	Captopril can interact regio- and stereo-specifically with various functional groups present at the active site of angiotensin converting enzyme (ACE). Since no X-ray structure of ACE is available, Captopril, as an ACE inhibitor may be used as a ‘molecular caliper’, to estimate upper and lower bound values for separation d, where the mercaptidic terminal group of the molecule is linked to the enzyme Zn2+ cofactor, while the carboxylate links via an hydrogen bond to the guanidine moiety of an arginine side chain. As the results of this Ab Initio study, the conformations of the dianionic form of the full captopril molecule are reported here.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::646af33ee06e9fbbe80a5e523681ce62 https://doi.org/10.1016/j.theochem.2003.08.084 Zobrazit plný text záznamu Full Text from ScienceDirect