
Discover Chemistry., Год журнала: 2025, Номер 2(1)
Опубликована: Май 9, 2025
Язык: Английский
Discover Chemistry., Год журнала: 2025, Номер 2(1)
Опубликована: Май 9, 2025
Язык: Английский
Journal of Peptide Science, Год журнала: 2025, Номер 31(6)
Опубликована: Апрель 27, 2025
ABSTRACT The secondary structure plays a crucial role in the biological activity of peptides. Various strategies have been developed to stabilize particular peptide conformations, including sequence modifications and macrocyclization approaches. Often, interplay between conformational constraint flexibility is central bioactivity. Here, we investigate how α‐helicity influences enzymatic head‐to‐tail cyclization using an engineered Sortase. We show that peptides with low helicity readily undergo intramolecular cyclization, while more rigid, helical exhibit complex behaviors cyclic dimer formation. These findings reveal increased rigidity can redirect reactions from intermolecular processes, demonstrates changes molecular guide chemical reactivity. insights advance design peptide‐derived materials, hydrogels, stimuli‐responsive probes.
Язык: Английский
Процитировано
0Discover Chemistry., Год журнала: 2025, Номер 2(1)
Опубликована: Май 9, 2025
Язык: Английский
Процитировано
0