PXD037525-1

PXD037525 is an original dataset announced via ProteomeXchange.

Title	Site-Selective Photocatalytic Functionalization of Peptides and Proteins at Selenocysteine
Description	The importance of modified peptides and proteins for applications in drug discovery, and for illuminating biological processes at the molecular level, has fueled 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 sitespecific functionalization of peptide and protein diselenides. This methodology, dubbed the photocatalytic diselenide contraction (PDC), 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 unprecedented photocatalytic transformation is proposed, which is supported by photoluminescence spectroscopy and density functional theory calculations. The utility of the PDC 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.
HostingRepository	PRIDE
AnnounceDate	2022-10-25
AnnouncementXML	Submission_2022-10-25_10:03:38.738.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	MarkLarance
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2022-10-18 08:02:09	ID requested
⏵ 1	2022-10-25 10:03:39	announced

Dataset with its publication pending

submitter keyword: Selenocysteine, modification

MarkLarance
contact affiliation	The University of Sydney
contact email	mark.larance@sydney.edu.au
lab head
MarkLarance
contact affiliation	The University of Sydney
contact email	mark.larance@sydney.edu.au
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2022/10/PXD037525

PRIDE project URI

• PRIDE
  1. PXD037525
     1. Label: PRIDE project
     2. Name: Site-Selective Photocatalytic Functionalization of Peptides and Proteins at Selenocysteine