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dc.contributor.authorDowman, L.J.-
dc.contributor.authorKulkarni, S.S.-
dc.contributor.authorAlegre-Requena, J.V.-
dc.contributor.authorGiltrap, A.M.-
dc.contributor.authorNorman, A.R.-
dc.contributor.authorSharma, A.-
dc.contributor.authorGallegos, L.C.-
dc.contributor.authorMackay, A.S.-
dc.contributor.authorWelegedara, A.P.-
dc.contributor.authorWatson, E.E.-
dc.contributor.authorvan Raad, D.-
dc.contributor.authorNiederacher, G.-
dc.contributor.authorHuhmann, S.-
dc.contributor.authorProschogo, N.-
dc.contributor.authorPatel, K.-
dc.contributor.authorLarance, M.-
dc.contributor.authorBecker, C.F.W.-
dc.contributor.authorMackay, J.P.-
dc.contributor.authorLakhwani, G.-
dc.contributor.authorHuber, T.-
dc.contributor.authoret al.-
dc.identifier.citationNature Communications, 2022; 13(1):6885-6885-
dc.description.abstractThe importance of modified peptides and proteins for applications in drug discovery, and for illuminating biological processes at the molecular level, is fueling a demand for efficient methods that facilitate the precise modification of these biomolecules. Herein, we describe the development of a photocatalytic method for the rapid and efficient dimerization and site-specific functionalization of peptide and protein diselenides. This methodology, dubbed the photocatalytic diselenide contraction, involves irradiation at 450 nm in the presence of an iridium photocatalyst and a phosphine and results in rapid and clean conversion of diselenides to reductively stable selenoethers. A mechanism for this photocatalytic transformation is proposed, which is supported by photoluminescence spectroscopy and density functional theory calculations. The utility of the photocatalytic diselenide contraction transformation is highlighted through the dimerization of selenopeptides, and by the generation of two families of protein conjugates via the site-selective modification of calmodulin containing the 21st amino acid selenocysteine, and the C-terminal modification of a ubiquitin diselenide.-
dc.description.statementofresponsibilityLuke J. Dowman, Sameer S. Kulkarni, Juan V. Alegre-Requena, Andrew M. Giltrap, Alexander R. Norman, Ashish Sharma, Liliana C. Gallegos, Angus S.Mackay, Adarshi P. Welegedara, Emma E. Watson, Damian van Raad, Gerhard Niederacher, Susanne Huhmann, Nicholas Proschogo, Karishma Patel, Mark Larance, Christian F. W. Becker, Joel P. Mackay, Girish Lakhwani, Thomas Huber, Robert S. Paton, Richard J. Payne-
dc.publisherSpringer Science and Business Media LLC-
dc.rights© The Author(s) 2022 This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit licenses/by/4.0/.-
dc.subjectAmino Acids-
dc.subject.meshAmino Acids-
dc.titleSite-selective photocatalytic functionalization of peptides and proteins at selenocysteine-
dc.typeJournal article-
dc.identifier.orcidWatson, E.E. [0000-0001-5946-473X]-
Appears in Collections:Physics publications

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