Selenoimidazolium Salts as Supramolecular Reagents for Protein Alkylation

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Selenoimidazolium Salts as Supramolecular Reagents for Protein Alkylation

JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)

ID	4614560
Author(s)	Lim, David; Wen, Xiaojin; Seebeck, Florian P.
Author(s) at UniBasel	Seebeck, Florian Peter
Year	2020
Title	Selenoimidazolium Salts as Supramolecular Reagents for Protein Alkylation
Journal	Chembiochem : a European journal of chemical biology
Volume	21
Number	24
Pages / Article-Number	3515-3520
Keywords	ergothioneine; methyltransferase; protein alkylation; selenoimidazole; selenoneine
Abstract	Se-benzyl selenoimidazolium salts are characterized by remarkable alkyl-transfer potential under physiological conditions. Structure-activity relationship studies show that selective monoalkylation of primary amines depends on supramolecular interactions between the selenoimidazole leaving group and the target nucleophile. We demonstrate that these reagents can be used for site-selective and nearly quantitative modification of the model protein lysozyme on Lys13, bypassing the higher intrinsic reactivities of Lys1 and Lys33. These observations introduce selenoimidazolium salts as novel class of electrophiles for selective N-alkylation of native proteins.
Publisher	Wiley
ISSN/ISBN	1439-4227 ; 1439-7633
edoc-URL	https://edoc.unibas.ch/81367/
Full Text on edoc	No
Digital Object Identifier DOI	10.1002/cbic.202000557
PubMed ID	http://www.ncbi.nlm.nih.gov/pubmed/32779842
Document type (ISI)	Journal Article

11/05/2024

Research Database / FORSCHUNGSDATENBANK