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A pH‐Induced Reversible Conformational Switch Able to Control the Photocurrent Efficiency in a Peptide Supramolecular System
Author(s) -
Kubitzky Sascha,
Venanzi Mariano,
Biondi Barbara,
Lettieri Raffaella,
De Zotti Marta,
Gatto Emanuela
Publication year - 2021
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202004527
Subject(s) - photocurrent , supramolecular chemistry , chemistry , peptide , helix (gastropod) , biophysics , electron transfer , conformational change , crystallography , photochemistry , stereochemistry , materials science , biochemistry , crystal structure , biology , optoelectronics , ecology , snail
External stimuli are potent tools that Nature uses to control protein function and activity. For instance, during viral entry and exit, pH variations are known to trigger large protein conformational changes. In Nature, also the electron transfer (ET) properties of ET proteins are influenced by pH‐induced conformational changes. In this work, a pH‐controlled, reversible 3 10 ‐helix to α‐helix conversion (from acidic to highly basic pH values and vice versa ) of a peptide supramolecular system built on a gold surface is described. The effect of pH on the ability of the peptide SAM to generate a photocurrent was investigated, with particular focus on the effect of the pH‐induced conformational change on photocurrent efficiency. The films were characterized by electrochemical and spectroscopic techniques, and were found to be very stable over time, also in contact with a solution. They were also able to generate current under illumination, with an efficiency that is the highest recorded so far with biomolecular systems.