Electrochemical Bioconjugation of Tryptophan Residues: A Strategy for Peptide Modification

Interest in electrocatalytic bioconjugation reactions has surged, particularly for modifying tryptophan and tyrosine residues in proteins. We used a cost-effective graphite felt electrode and low-current methodology to achieve selective bioconjugation of tryptophan with thiophenols, yielding up to 9...

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Bibliographic Details
Published in:Organic letters 2024-07, Vol.26 (26), p.5447-5452
Main Authors: Wan, Chenggang, Sun, Rong, Xia, Wenjie, Jiang, Haoyang, Chen, Bo-Xun, Kuo, Pei-Chi, Zhang, Wan-Rou, Yang, Guichun, Li, Dingyu, Chiang, Chien-Wei, Weng, Yue
Format: Article
Language:English
Subjects:
chemical bonding
cost effectiveness
Electrochemical Techniques
electrochemistry
Electrodes
graphene
Molecular Structure
Peptides - chemistry
Peptides, Cyclic - chemistry
polypeptides
Somatostatin - analogs & derivatives
Somatostatin - chemistry
therapeutics
tryptophan
Tryptophan - chemistry
tyrosine
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Summary:Interest in electrocatalytic bioconjugation reactions has surged, particularly for modifying tryptophan and tyrosine residues in proteins. We used a cost-effective graphite felt electrode and low-current methodology to achieve selective bioconjugation of tryptophan with thiophenols, yielding up to 92%. This method exclusively labeled tryptophan residues and incorporated fluorinated tryptophan for NMR analysis. Eight polypeptides, including lanreotide and leuprorelin, were effectively coupled, demonstrating the method’s versatility and potential for novel diagnostic and therapeutic agents.
ISSN:1523-7060
1523-7052
1523-7052
DOI:10.1021/acs.orglett.4c01662