Peptide 2-formylthiophenol esters do not proceed through a Ser/Thr ligation pathway, but participate in a peptide aminolysis to enable peptide condensation and cyclization

Chun Ling Tung; Clarence T T Wong; Xuechen Li

doi:10.1039/c5ob00825e

Peptide 2-formylthiophenol esters do not proceed through a Ser/Thr ligation pathway, but participate in a peptide aminolysis to enable peptide condensation and cyclization

Org Biomol Chem. 2015 Jul 7;13(25):6922-6. doi: 10.1039/c5ob00825e. Epub 2015 May 27.

Authors

Chun Ling Tung¹, Clarence T T Wong, Xuechen Li

Affiliation

¹ Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong, China. [email protected].

PMID: 26013965
DOI: 10.1039/c5ob00825e

Abstract

Peptide thiol salicylaldehyde (SAL) esters unexpectedly do not follow a Ser/Thr ligation pathway to react with peptides containing N-terminal Ser/Thr, but proceed towards a peptide aminolysis in DMSO. The reaction takes place even at a low substrate concentration (1 mM). The method has been successfully used to synthesize several natural cyclic peptides, with a high ratio of monocyclic to dimeric products.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Aldehydes / chemistry*
Amines / chemistry*
Amino Acid Sequence
Cyclization
Dimethyl Sulfoxide / chemistry
Esters / chemistry
Molecular Sequence Data
Peptides / chemistry*
Peptides, Cyclic / chemical synthesis*
Peptides, Cyclic / chemistry
Phenols / chemistry*
Sulfhydryl Compounds / chemistry*

Substances

Aldehydes
Amines
Esters
Peptides
Peptides, Cyclic
Phenols
Sulfhydryl Compounds
salicylaldehyde
thiophenol
Dimethyl Sulfoxide