Work

Oxidative Deselenization of Selenocysteine: Applications for Programmed Ligation at Serine

Year: 2015

Type: article

Abstract: Despite the unique chemical properties of selenocysteine (Sec), ligation at Sec is an under-utilized methodology for protein synthesis. We describe herein an unprecedented protocol for the conversion of Sec to serine (Ser) in a single, high-yielding step. When coupled with ligation at Sec, this transformation provides a new approach to programmed ligations at Ser residues. This new reaction is compatible with a wide range of functionality, including the presence of unprotected amino acid side chains and appended glycans. The utility of the methodology is demonstrated in the rapid synthesis of complex glycopeptide fragments of the epithelial glycoproteins MUC5AC and MUC4 and through the total synthesis of the structured, cysteine (Cys)-free protein eglin C.

Source: Angewandte Chemie International Edition

DOI: 10.1002/anie.201504639

Authors: Lara R. Malins, Nicholas J. Mitchell, Sheena McGowan, Richard J. Payne

Institutions: The University of Sydney, Monash University

Language: English

Topic: Chemical Synthesis and Analysis

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: Australian Research Council

Award: Development and application of new peptide ligation methods for the synthesis and structure-function studies of glycoproteins