Helical foldamers incorporating photoswitchable residues for light-mediated modulation of conformational preference

Daniela Mazzier, Marco Crisma, Matteo De Poli, Giulia Marafon, Cristina Peggion, Jonathan Clayden*, Alessandro Moretto

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)

26 Citations (Scopus)
284 Downloads (Pure)

Abstract

An E unsaturated fumaramide linkage may be introduced into Aib peptide foldamer structures by standard coupling methods and photoisomerized to its Z (maleamide) isomer by irradiation with UV light. As a result of the photoisomerization, a new hydrogen-bonded contact becomes possible between the peptide domains located on either side of the unsaturated linkage. Using the fumaramide/maleamide linker to couple a chiral and an achiral fragment allows the change in hydrogen bond network to communicate a conformational preference, inducing a screw sense preference in the achiral domain of the maleamide-linked foldamers that is absent from the fumaramides. Evidence for the induced screw sense preference is provided by NMR and CD, and also by the turning on by light of the diastereoselectivity of a peptide chain extension reaction. The fumaramide/maleamide linker thus acts as a "conformational photodiode" that conducts stereochemical information as a result of irradiation by UV light.
Original languageEnglish
Pages (from-to)8007-8018
Number of pages12
JournalJournal of the American Chemical Society
Volume138
Issue number25
Early online date3 Jun 2016
DOIs
Publication statusPublished - 29 Jun 2016

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