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Article: Structure-Activity Relationship Studies of N- and C-Terminally Modified Secretin Analogs for the Human Secretin Receptor

TitleStructure-Activity Relationship Studies of N- and C-Terminally Modified Secretin Analogs for the Human Secretin Receptor
Authors
Issue Date2016
PublisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.action
Citation
Plos One, 2016, v. 11 n. 3, p. e0149359 How to Cite?
AbstractThe pleiotropic role of human secretin (hSCT) validates its potential use as a therapeutic agent. Nevertheless, the structure of secretin in complex with its receptor is necessary to develop a suitable therapeutic agent. Therefore, in an effort to design a three-dimensional virtual homology model and identify a peptide agonist and/or antagonist for the human secretin receptor (hSR), the significance of the primary sequence of secretin peptides in allosteric binding and activation was elucidated using virtual docking, FRET competitive binding and assessment of the cAMP response. Secretin analogs containing various N- or C-terminal modifications were prepared based on previous findings of the role of these domains in receptor binding and activation. These analogs exhibited very low or no binding affinity in a virtual model, and were found to neither exhibit in vitro binding nor agonistic or antagonistic properties. A parallel analysis of the analogs in the virtual model and in vitro studies revealed instability of these peptide analogs to bind and activate the receptor.
Persistent Identifierhttp://hdl.handle.net/10722/227858
ISSN
2023 Impact Factor: 2.9
2023 SCImago Journal Rankings: 0.839
ISI Accession Number ID
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Errata

 

DC FieldValueLanguage
dc.contributor.authorSingh, K-
dc.contributor.authorSenthil, V-
dc.contributor.authorArokiaraj, AWR-
dc.contributor.authorLeprince, J-
dc.contributor.authorLefranc, B-
dc.contributor.authorVaudry, D-
dc.contributor.authorAllam, AA-
dc.contributor.authorAjarem, J-
dc.contributor.authorChow, BKC-
dc.date.accessioned2016-07-20T07:46:26Z-
dc.date.available2016-07-20T07:46:26Z-
dc.date.issued2016-
dc.identifier.citationPlos One, 2016, v. 11 n. 3, p. e0149359-
dc.identifier.issn1932-6203-
dc.identifier.urihttp://hdl.handle.net/10722/227858-
dc.description.abstractThe pleiotropic role of human secretin (hSCT) validates its potential use as a therapeutic agent. Nevertheless, the structure of secretin in complex with its receptor is necessary to develop a suitable therapeutic agent. Therefore, in an effort to design a three-dimensional virtual homology model and identify a peptide agonist and/or antagonist for the human secretin receptor (hSR), the significance of the primary sequence of secretin peptides in allosteric binding and activation was elucidated using virtual docking, FRET competitive binding and assessment of the cAMP response. Secretin analogs containing various N- or C-terminal modifications were prepared based on previous findings of the role of these domains in receptor binding and activation. These analogs exhibited very low or no binding affinity in a virtual model, and were found to neither exhibit in vitro binding nor agonistic or antagonistic properties. A parallel analysis of the analogs in the virtual model and in vitro studies revealed instability of these peptide analogs to bind and activate the receptor.-
dc.languageeng-
dc.publisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.action-
dc.relation.ispartofPLoS ONE-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleStructure-Activity Relationship Studies of N- and C-Terminally Modified Secretin Analogs for the Human Secretin Receptor-
dc.typeArticle-
dc.identifier.emailChow, BKC: bkcc@hkusua.hku.hk-
dc.identifier.authorityChow, BKC=rp00681-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1371/journal.pone.0149359-
dc.identifier.pmid26930505-
dc.identifier.scopuseid_2-s2.0-84961924310-
dc.identifier.hkuros270766-
dc.identifier.volume11-
dc.identifier.issue3-
dc.identifier.spagee0149359-
dc.identifier.epagee0149359-
dc.identifier.isiWOS:000371434500025-
dc.publisher.placeUnited States-
dc.relation.erratumdoi:10.1371/journal.pone.0165770-
dc.relation.projectStrategic research of hormones and their receptors in the water homeostatic axis: from molecular mechanisms to anti-hypertensive drug design-
dc.relation.projectThe Concerted Actions of Secretin with Vasopressin in Salt Conservation-
dc.identifier.issnl1932-6203-

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