Tryptophan in Multicomponent Petasis Reactions for Peptide Stapling and Late-Stage Functionalisation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F23%3A73620842" target="_blank" >RIV/61989592:15310/23:73620842 - isvavai.cz</a>
Result on the web
<a href="https://onlinelibrary.wiley.com/doi/epdf/10.1002/anie.202307782" target="_blank" >https://onlinelibrary.wiley.com/doi/epdf/10.1002/anie.202307782</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/anie.202307782" target="_blank" >10.1002/anie.202307782</a>
Alternative languages
Result language
angličtina
Original language name
Tryptophan in Multicomponent Petasis Reactions for Peptide Stapling and Late-Stage Functionalisation
Original language description
Peptide stapling is a robust strategy for generating enzymatically stable, macrocyclic peptides. The incorporation of biologically relevant tags(such as cell-penetrating motifs or fluorescent dyes) into peptides, while preserving their binding interactions and enhancing their stability, is highly sought after. Consequently, the quest for novel peptide stapling methodologies that would easily incorporate such motifs, remains eminent. Despite the unique opportunities offered by tryptophan’s indole scaffold for targeted functionalisation, its utilisation in peptide stapling waslimited comparedto other amino acids. Herein, we present an unprecedentedapproach for peptide stapling using the tryptophan-mediated Petasis reaction(TMPR). This method represents a versatile tool for the synthesis of both stapled and labelled peptides, applicable to both solution and solid-phase synthesis. Importantly, the utilisation of the Petasis reaction in combinationwith tryptophan represents a significant advancementin the field of peptide stapling, facilitating the formation of stapled peptides in one straightforward, multicomponent fashion, while circumventing formation of undesired by-products –a persistent challenge in current methodologies. Furthermore, this approach allows forefficient and diverse late-stage peptide modifications, thereby enablingrapid production of numerous conjugates for biological and medicinal applications.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10401 - Organic chemistry
Result continuities
Project
<a href="/en/project/GN22-07138O" target="_blank" >GN22-07138O: Conformationally-constrained peptide-drug conjugates as a platform for targeted therapeutics</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
ISSN
1433-7851
e-ISSN
1521-3773
Volume of the periodical
62
Issue of the periodical within the volume
34
Country of publishing house
DE - GERMANY
Number of pages
9
Pages from-to
"e202307782-1"-"e202307782-9"
UT code for WoS article
001027654300001
EID of the result in the Scopus database
2-s2.0-85164694874