Jump to main content
Jump to site search


Native chemical ligation at methionine bioisostere norleucine allows for N-terminal chemical protein ligation

Abstract

The development of γ-thionorleucine (ThioNle) as handle for native chemical ligation-desulfurization is reported here. ThioNle is a new addition to the expanding thiolated amino acid toolbox and serves as methionine substitute in NCL with the advantage that it lacks the undesirable oxidation-prone thioether moiety. Its usefulness for N-terminal ubiquitination is demonstrated by efficient preparation of fully synthetic linear diubiquitin with preserved protein folding compared to expressed material. Interestingly, gel-based deubiquitinating assays revealed that the methioinine to norleucine subtsitution did affect diubiquitin cleavage, which may indicate a more profound role for methionine in the interaction between ubiquitin and the deubiquitinating enzymes than has been known so far.

Back to tab navigation

Supplementary files

Publication details

The article was received on 10 Jul 2018, accepted on 09 Aug 2018 and first published on 09 Aug 2018


Article type: Paper
DOI: 10.1039/C8OB01627E
Citation: Org. Biomol. Chem., 2018, Accepted Manuscript
  •   Request permissions

    Native chemical ligation at methionine bioisostere norleucine allows for N-terminal chemical protein ligation

    P. P. Geurink, H. Ovaa, B. Xin and B. D.M. van Tol, Org. Biomol. Chem., 2018, Accepted Manuscript , DOI: 10.1039/C8OB01627E

Search articles by author

Spotlight

Advertisements