C–H olefination of tryptophan residues in peptides: control of residue selectivity and peptide–amino acid cross-linking

Terrey, M.J., Holmes, A., Perry, C.C. ORCID: 0000-0003-1517-468X and Cross, W.B. ORCID: 0000-0001-6277-400X, 2019. C–H olefination of tryptophan residues in peptides: control of residue selectivity and peptide–amino acid cross-linking. Organic Letters, 21 (19), pp. 7902-7907. ISSN 1523-7060

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Abstract

There is high demand for new methods to modify peptides, for application in drug discovery and biomedicine. A C–H functionalization protocol for the olefination of tryptophan residues in peptides is described. The modification is successful for Trp residues at any position in the peptide, has broad scope in the styrene coupling partner, and offers opportunities for conjugating peptides with other biomolecules. For peptides containing both Trp and Phe, directing group manipulation enables full control of residue selectivity.

Item Type:	Journal article
Publication Title:	Organic Letters
Creators:	Terrey, M.J., Holmes, A., Perry, C.C. and Cross, W.B.
Publisher:	American Chemical Society
Date:	4 October 2019
Volume:	21
Number:	19
ISSN:	1523-7060
Identifiers:	Number Type 10.1021/acs.orglett.9b02894 DOI
Divisions:	Schools > School of Science and Technology
Record created by:	Jonathan Gallacher
Date Added:	16 Sep 2019 15:27
Last Modified:	31 May 2021 15:17
URI:	https://irep.ntu.ac.uk/id/eprint/37676

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