The design of a dipeptide library for screening at peptide receptor sites

Autor:	William Howson, David Christopher Horwell, Ratcliffe Giles S, David C. Rees
Rok vydání:	1993
Předmět:	chemistry.chemical_classification Dipeptide Peptide receptor Stereochemistry Organic Chemistry Clinical Biochemistry Pharmaceutical Science Biochemistry Combinatorial chemistry Amino acid chemistry.chemical_compound chemistry Drug Discovery Molecular Medicine Molecular Biology
Zdroj:	Bioorganic & Medicinal Chemistry Letters. 3:799-802
ISSN:	0960-894X
DOI:	10.1016/s0960-894x(00)80669-1
Popis:	A physico-chemical information rich library of 256 N-protected dipeptides is described. This library has been constructed using a factorial design in the principal properties of the amino acids. These compounds represent a data set of diverse physical properties which can be screened against a variety of protein substrates in binding assays in the search for micromolar chemical leads for drug design. The concept is supported by the design of CCK-A and -B non-peptide ligands from the dipeptide lead Boc-Trp-Phe-NH2, a non-contiguous dipeptide fragment of CCK.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::19e50da6aed587824b077c40242f7402 https://doi.org/10.1016/s0960-894x(00)80669-1 Zobrazit plný text záznamu