Potent complement C3a receptor agonists derived from oxazole amino acids: Structure-activity relationships

Autor:	Mei-Kwan Yau, Jacky Y. Suen, David P. Fairlie, Anthony N. Reed, Conor C G Scully, Ranee Singh, Thomas Durek, Peifei Chu, Robert Reid
Rok vydání:	2015
Předmět:	Agonist medicine.drug_class Clinical Biochemistry Pharmaceutical Science chemical and pharmacologic phenomena Peptide Tripeptide 010402 general chemistry Arginine Ligands 01 natural sciences Biochemistry Serine 03 medical and health sciences chemistry.chemical_compound Structure-Activity Relationship Drug Discovery medicine Humans Amino Acids Benzhydryl Compounds Molecular Biology Oxazoles 030304 developmental biology Oxazole chemistry.chemical_classification 0303 health sciences biology Dose-Response Relationship Drug Molecular Structure Chemistry Macrophages Organic Chemistry Dipeptides 0104 chemical sciences 3. Good health Amino acid Receptors Complement biology.protein Molecular Medicine C3a receptor Leucine
Zdroj:	Bioorganicmedicinal chemistry letters. 25(23)
ISSN:	1464-3405
Popis:	Potent ligands for the human complement C3a receptor (C3aR) were developed from the almost inactive tripeptide Leu-Ala-Arg corresponding to the three C-terminal residues of the endogenous peptide agonist C3a. The analogous Leu-Ser-Arg was modified by condensing the serine side chain with the leucine carbonyl with elimination of water to form leucine-oxazole-arginine. Subsequent elaboration with a variety of N-terminal amide capping groups produced agonists as potent as human C3a itself in stimulating Ca(2+) release from human macrophages. Structure-activity relationships are discussed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dca85cef21d72282fa5da9f17b6dafd https://pubmed.ncbi.nlm.nih.gov/26522948 Zobrazit plný text záznamu Full Text from ScienceDirect