Structure and activity of NO synthase inhibitors specific to the L-arginine binding site

Autor:	A. A. Mandrugin, V.G. Skvortsov, V. M. Fedoseev, S. Ya. Proskuryakov, A. G. Konoplyannikov
Rok vydání:	2005
Předmět:	chemistry.chemical_classification Arginine Stereochemistry Biophysics Peptide General Medicine Biochemistry Genetics and Molecular Biology (miscellaneous) Biochemistry Amino acid chemistry.chemical_compound Enzyme chemistry Geriatrics and Gerontology Binding site Arginine binding Guanidine Heme
Zdroj:	Biochemistry (Moscow). 70:8-23
ISSN:	1608-3040 0006-2979
DOI:	10.1007/s10541-005-0048-9
Popis:	Synthesis of compounds containing a fragment similar to the guanidine group of L-arginine, which is a substrate of nitric oxide synthase (NOS), is the main direction in creating NOS inhibitors. The inhibitory effect of such compounds is caused not only by their competition with the substrate for the L-arginine-binding site and/or oxidizing center of the enzyme (heme) but also by interaction with peptide motifs of the enzyme that influence its dimerization, affinity for cofactors, and interaction with associated proteins. Structures, activities, and relative in vitro and in vivo specificities of various NOS inhibitors (amino acid and non-amino acid) with linear or cyclic structure and containing guanidine, amidine, or isothiuronium group are considered. These properties are mainly analyzed by comparison with effects of the inhibitors on the inducible NOS.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::343ba673ba39e1d4976cd2f25676c7b2 https://doi.org/10.1007/s10541-005-0048-9 Zobrazit plný text záznamu Plný text ve formátu PDF