Peptide Stapling through Site-Directed Conjugation of Triazine Moieties to the Tyrosine Residues of a Peptide
Yue Zhang, Ruijuan Yin, Hao Jiang, Chaoming Wang, Xiao Wang, Dongping Wang, Kai Zhang, Rilei Yu, Xuechen Li, Tao Jiang
Abstract
Peptide stapling is a strategy for improving the biological properties of peptides. Herein, we report a novel method for stapling peptides that utilizes bifunctional triazine moieties for two-component conjugation to the phenolic hydroxyl groups of tyrosine, which enables efficient stapling of unprotected peptides. In addition, we applied this strategy to the RGD peptide that can target integrins and demonstrated that the stapled RGD peptide had significantly improved plasma stability and integrin-targeting ability.
Topics & Concepts
ChemistryPeptideTyrosineBifunctionalIntegrinTriazineCombinatorial chemistryStereochemistryBiochemistryPolymer chemistryReceptorCatalysisChemical Synthesis and AnalysisClick Chemistry and ApplicationsMonoclonal and Polyclonal Antibodies Research