Home > Research Progress > Li group published article on Bioconjugate Chemistry about a study of dual in-tether chiral centers modulate peptide helicity


The facile chemical modification on the peptide cross-linking moiety is an important strategy to improve the physicochemical properties of a peptide. Herein, peptides were contrained into helical conformations via the synergistic effects of dual in-tether chiral centers. A pentapeptide minimalistic model was used to determine the correlation between the absolute configurations of the dual in-tether chiral centers and the secondary structures of the peptides. This strategy provides an on-tether modification site that does not interrupt the secondary structure of the peptide