Various modifications of the amphipathic dynorphin A pharmacophore for rat brain bradykinin receptors

Autor:	Frank Porreca, Victor J. Hruby, Michael Remesic, Christopher Chan, David Rankin, Cyf Ramos-Colon, Yeon Sun Lee, Robert Kupp, Sara M. Hall, Josephine Lai
Rok vydání:	2016
Předmět:	Bradykinin Dynorphin Pharmacology Ligands 010402 general chemistry Dynorphins 01 natural sciences Biochemistry Article Inhibitory Concentration 50 Structure-Activity Relationship 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Drug Discovery Animals Structure–activity relationship Bradykinin receptor Receptor Endogenous opioid Chemistry Receptors Bradykinin Organic Chemistry Dynorphin A Rats 0104 chemical sciences Cell biology nervous system Molecular Medicine Pharmacophore 030217 neurology & neurosurgery
Zdroj:	Chemical Biology & Drug Design. 88:615-619
ISSN:	1747-0277
Popis:	As a unique endogenous opioid ligand, dynorphin A shows paradoxical neuroexcitatory effects at bradykinin receptors, and the effects are known to be amplified by the upregulation of dynorphin A under chronic pain and inflammatory conditions. In our earlier structure-activity relationship studies, the amphipathic dynorphin A fragment, [Des-Arg(7) ]-Dyn A-(4-11), was identified as a pharmacophore for the bradykinin receptors along with key structural features. Here, further modifications of the pharmacophore showed that the position of a Pro residue is also an important feature because of its role in making (or disrupting) a β-turn or 310 helix structure which is crucial for receptor recognition.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7271ba4894aa7fe3dfedfc130ddf9e18 https://doi.org/10.1111/cbdd.12789 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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