Synthetic cysteine-based tools for probing protein posttranslational modifications

Jordi C. J. Hintzen*, Jasmin Mecinović*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

38 Downloads (Pure)

Abstract

Posttranslational modifications (PTMs) are naturally occurring chemical modifications of proteins that influence their structure, function and dynamics. Probing the role of specific PTMs remains a challenge due to the complex molecular language that regulates PTMs. Cysteine, one of the twenty proteinogenic amino acids, displays a unique reactivity that can be employed for site-specific introduction of diverse mimics of naturally occurring amino acids possessing PTMs. Cysteine-based methods are often synthetically facile and cysteine residues can be easily introduced into proteins by site-directed mutagenesis. In this digest article we provide an overview of recently developed synthetic methods for preparation of mimics of posttranslationally modified amino acids directly via cysteine or indirectly via dehydroalanine.
Original languageEnglish
Article number154602
JournalTetrahedron Letters
Volume124
Number of pages10
ISSN0040-4039
DOIs
Publication statusPublished - 11. Jul 2023

Fingerprint

Dive into the research topics of 'Synthetic cysteine-based tools for probing protein posttranslational modifications'. Together they form a unique fingerprint.

Cite this