Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/131378
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dc.contributor.author | Horsfall, A.J. | - |
dc.contributor.author | McDougal, D.P. | - |
dc.contributor.author | Scanlon, D.B. | - |
dc.contributor.author | Bruning, J.B. | - |
dc.contributor.author | Abell, A.D. | - |
dc.date.issued | 2021 | - |
dc.identifier.citation | ChemBioChem: a European journal of chemical biology, 2021; 22(17):2711-2720 | - |
dc.identifier.issn | 1439-4227 | - |
dc.identifier.issn | 1439-7633 | - |
dc.identifier.uri | http://hdl.handle.net/2440/131378 | - |
dc.description | First published: 09 June 2021 | - |
dc.description.abstract | An i-i+4 or i-i+3 bimane-containing linker was introduced into a peptide known to target Estrogen Receptor alpha (ERα) in order to stabilise an α-helical geometry. These macrocycles were studied by CD and NMR to reveal the i-i+4 constrained peptide adopts a 310-helical structure in solution, and an α-helical conformation on interaction with the ERα coactivator recruitment surface in silico. An acyclic bimane-modified peptide is also helical, when it includes a tryptophan or tyrosine residue; but is significantly less helical with a phenylalanine or alanine residue, which indicates such a bimane modification influences peptide structure in a sequence dependent manner. The fluorescence intensity of the bimane appears influenced by peptide conformation, where helical peptides displayed a fluorescence increase when TFE was added to phosphate buffer, compared to a decrease for less helical peptides. This study presents the bimane as a useful modification to influence peptide structure as an acyclic peptide modification, or as a side-chain constraint to give a macrocycle. | - |
dc.description.statementofresponsibility | Aimee J. Horsfall, Daniel P. McDougal, Denis B. Scanlon, John B. Bruning, Andrew D. Abell | - |
dc.language.iso | en | - |
dc.publisher | Wiley | - |
dc.rights | © 2021 Wiley-VCH GmbH | - |
dc.source.uri | http://dx.doi.org/10.1002/cbic.202100241 | - |
dc.subject | Bimane | - |
dc.subject | Helical structures | - |
dc.subject | Peptidomimetics | - |
dc.subject | fluorescence | - |
dc.subject | peptides | - |
dc.title | Approaches to introduce helical structure in cysteine-containing peptides with a bimane group | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1002/cbic.202100241 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/CE140100003 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Horsfall, A.J. [0000-0003-1276-2742] | - |
dc.identifier.orcid | McDougal, D.P. [0000-0003-4499-6789] | - |
dc.identifier.orcid | Bruning, J.B. [0000-0002-6919-1824] | - |
dc.identifier.orcid | Abell, A.D. [0000-0002-0604-2629] | - |
Appears in Collections: | Aurora harvest 8 Pharmacology publications |
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