Visible-Light-Driven Fluoroalkylation of Tryptophan Residues in Peptides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F20%3A43920929" target="_blank" >RIV/60461373:22340/20:43920929 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/21:00540179 RIV/60461373:22340/21:43920929 RIV/00216208:11310/21:10439273

Výsledek na webu

<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cptc.202000214" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cptc.202000214</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/cptc.202000214" target="_blank" >10.1002/cptc.202000214</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Visible-Light-Driven Fluoroalkylation of Tryptophan Residues in Peptides

Popis výsledku v původním jazyce

Trifluoromethylated and fluoroalkylated cyclic λ3-iodanes and their acyclic salts were used for visible light-driven fluoroalkylation of tryptophan and tryptophan-containing peptides in aqueous media. In comparison to previously reported fluoroalkylation using similar reagents and sodium ascorbate as reductant, the photochemical process did not require any additive or catalyst and was more selective for Trp versus other aromatic amino acids due to the gradual production of fluoroalkyl radicals over the whole irradiation period. However, in the presence of Cys residues, both methods were not selective and cysteine sulfhydryl groups were fluoroalkylated in side reactions. Spectroscopic and photochemical investigations as well as quantum chemical calculations provided insight into the reaction mechanism. The process was found to be photoinduced involving the formation of fluoroalkyl radical from the excited state of λ3-iodane. © 2020 Wiley-VCH GmbH

Název v anglickém jazyce

Visible-Light-Driven Fluoroalkylation of Tryptophan Residues in Peptides

Popis výsledku anglicky

Trifluoromethylated and fluoroalkylated cyclic λ3-iodanes and their acyclic salts were used for visible light-driven fluoroalkylation of tryptophan and tryptophan-containing peptides in aqueous media. In comparison to previously reported fluoroalkylation using similar reagents and sodium ascorbate as reductant, the photochemical process did not require any additive or catalyst and was more selective for Trp versus other aromatic amino acids due to the gradual production of fluoroalkyl radicals over the whole irradiation period. However, in the presence of Cys residues, both methods were not selective and cysteine sulfhydryl groups were fluoroalkylated in side reactions. Spectroscopic and photochemical investigations as well as quantum chemical calculations provided insight into the reaction mechanism. The process was found to be photoinduced involving the formation of fluoroalkyl radical from the excited state of λ3-iodane. © 2020 Wiley-VCH GmbH

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ChemPhotoChem

ISSN

2367-0932

e-ISSN

—

Svazek periodika

5

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

9

Strana od-do

43-50

Kód UT WoS článku

000572506800001

EID výsledku v databázi Scopus

2-s2.0-85091459109