Visible-Light-Driven Fluoroalkylation of Tryptophan Residues in Peptides

0540179 - ÚOCHB 2022 RIV DE eng J - Journal Article
Rahimidashaghoul, Kheironnesae - Klimánková, Iveta - Hubálek, Martin - Matoušek, V. - Filgas, Josef - Slavíček, P. - Slanina, Tomáš - Beier, Petr
Visible-Light-Driven Fluoroalkylation of Tryptophan Residues in Peptides.
ChemPhotoChem. Roč. 5, č. 1 (2021), s. 43-50. ISSN 2367-0932. E-ISSN 2367-0932
R&D Projects: GA ČR(CZ) GA17-00598S; GA ČR(CZ) GJ19-20467Y
Institutional support: RVO:61388963
Keywords : bioconjugation * fluoroalkylation * iodanes * peptides * radical reactions
OECD category: Organic chemistry
Impact factor: 3.679, year: 2021
Method of publishing: Limited access
https://doi.org/10.1002/cptc.202000214

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.
Permanent Link: http://hdl.handle.net/11104/0317823