A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch
The insertion of azobenzene moiety in complex molecular protein or peptide systems can lead to molecular switches to be used to determine kinetics of folding/unfolding properties of secondary structures, such as α-helix, β-turn, or β-hairpin. In fact, in azobenzene, absorption of light induces a rev...
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doaj-0334c1bf059047889ec79a8e8a6fb43f2020-11-25T02:26:01ZengFrontiers Media S.A.Frontiers in Chemistry2296-26462019-03-01710.3389/fchem.2019.00180447532A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational SwitchFrancesca Nuti0Francesca Nuti1Cristina Gellini2Maud Larregola3Lorenzo Squillantini4Lorenzo Squillantini5Riccardo Chelli6Riccardo Chelli7Pier Remigio Salvi8Olivier Lequin9Giangaetano Pietraperzia10Giangaetano Pietraperzia11Anna Maria Papini12Anna Maria Papini13Anna Maria Papini14Laboratory of Peptide and Protein Chemistry and Biology (PeptLab), Sesto Fiorentino, ItalyDepartment of Chemistry “Ugo Schiff”, University of Florence, Sesto Fiorentino, ItalyDepartment of Chemistry “Ugo Schiff”, University of Florence, Sesto Fiorentino, ItalyPeptLab@UCP Platform and Laboratory of Chemical Biology EA4505, Université Paris-Seine, Cergy-Pontoise, FranceLaboratory of Peptide and Protein Chemistry and Biology (PeptLab), Sesto Fiorentino, ItalyDepartment of Chemistry “Ugo Schiff”, University of Florence, Sesto Fiorentino, ItalyDepartment of Chemistry “Ugo Schiff”, University of Florence, Sesto Fiorentino, ItalyEuropean Laboratory for Non-Linear Spectroscopy (LENS), Sesto Fiorentino, ItalyDepartment of Chemistry “Ugo Schiff”, University of Florence, Sesto Fiorentino, ItalyLaboratory of Biomolecules, CNRS, Sorbonne University, Ecole Normale Superieure, PSL University, Paris, FranceDepartment of Chemistry “Ugo Schiff”, University of Florence, Sesto Fiorentino, ItalyEuropean Laboratory for Non-Linear Spectroscopy (LENS), Sesto Fiorentino, ItalyLaboratory of Peptide and Protein Chemistry and Biology (PeptLab), Sesto Fiorentino, ItalyDepartment of Chemistry “Ugo Schiff”, University of Florence, Sesto Fiorentino, ItalyPeptLab@UCP Platform and Laboratory of Chemical Biology EA4505, Université Paris-Seine, Cergy-Pontoise, FranceThe insertion of azobenzene moiety in complex molecular protein or peptide systems can lead to molecular switches to be used to determine kinetics of folding/unfolding properties of secondary structures, such as α-helix, β-turn, or β-hairpin. In fact, in azobenzene, absorption of light induces a reversible trans ↔ cis isomerization, which in turns generates a strain or a structure relaxation in the chain that causes peptide folding/unfolding. In particular azobenzene may permit reversible conformational control of hairpin formation. In the present work a synthetic photochromic azobenzene amino acid derivative was incorporated as a turn element to modify the synthetic peptide [Pro7,Asn8,Thr10]CSF114 previously designed to fold as a type I β-turn structure in biomimetic HFA/water solution. In particular, the P-N-H fragment at positions 7–9, involved in a β-hairpin, was replaced by an azobenzene amino acid derivative (synthesized ad hoc) to investigate if the electronic properties of the novel peptidomimetic analog could induce variations in the isomerization process. The absorption spectra of the azopeptidomimetic analog of the type I β-turn structure and of the azobenzene amino acid as control were measured as a function of the irradiation time exciting into the respective first ππ* and nπ* transition bands. Isomerization of the azopeptidomimetic results strongly favored by exciting into the ππ* transition. Moreover, conformational changes induced by the cis↔ trans azopeptidomimetic switch were investigated by NMR in different solvents.https://www.frontiersin.org/article/10.3389/fchem.2019.00180/fullazobenzenecis/trans photoisomerizationphotoswitchable peptideoptical controlNMR spectroscopyUV/Vis spectroscopy |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Francesca Nuti Francesca Nuti Cristina Gellini Maud Larregola Lorenzo Squillantini Lorenzo Squillantini Riccardo Chelli Riccardo Chelli Pier Remigio Salvi Olivier Lequin Giangaetano Pietraperzia Giangaetano Pietraperzia Anna Maria Papini Anna Maria Papini Anna Maria Papini |
spellingShingle |
Francesca Nuti Francesca Nuti Cristina Gellini Maud Larregola Lorenzo Squillantini Lorenzo Squillantini Riccardo Chelli Riccardo Chelli Pier Remigio Salvi Olivier Lequin Giangaetano Pietraperzia Giangaetano Pietraperzia Anna Maria Papini Anna Maria Papini Anna Maria Papini A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch Frontiers in Chemistry azobenzene cis/trans photoisomerization photoswitchable peptide optical control NMR spectroscopy UV/Vis spectroscopy |
author_facet |
Francesca Nuti Francesca Nuti Cristina Gellini Maud Larregola Lorenzo Squillantini Lorenzo Squillantini Riccardo Chelli Riccardo Chelli Pier Remigio Salvi Olivier Lequin Giangaetano Pietraperzia Giangaetano Pietraperzia Anna Maria Papini Anna Maria Papini Anna Maria Papini |
author_sort |
Francesca Nuti |
title |
A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch |
title_short |
A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch |
title_full |
A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch |
title_fullStr |
A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch |
title_full_unstemmed |
A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch |
title_sort |
photochromic azobenzene peptidomimetic of a β-turn model peptide structure as a conformational switch |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Chemistry |
issn |
2296-2646 |
publishDate |
2019-03-01 |
description |
The insertion of azobenzene moiety in complex molecular protein or peptide systems can lead to molecular switches to be used to determine kinetics of folding/unfolding properties of secondary structures, such as α-helix, β-turn, or β-hairpin. In fact, in azobenzene, absorption of light induces a reversible trans ↔ cis isomerization, which in turns generates a strain or a structure relaxation in the chain that causes peptide folding/unfolding. In particular azobenzene may permit reversible conformational control of hairpin formation. In the present work a synthetic photochromic azobenzene amino acid derivative was incorporated as a turn element to modify the synthetic peptide [Pro7,Asn8,Thr10]CSF114 previously designed to fold as a type I β-turn structure in biomimetic HFA/water solution. In particular, the P-N-H fragment at positions 7–9, involved in a β-hairpin, was replaced by an azobenzene amino acid derivative (synthesized ad hoc) to investigate if the electronic properties of the novel peptidomimetic analog could induce variations in the isomerization process. The absorption spectra of the azopeptidomimetic analog of the type I β-turn structure and of the azobenzene amino acid as control were measured as a function of the irradiation time exciting into the respective first ππ* and nπ* transition bands. Isomerization of the azopeptidomimetic results strongly favored by exciting into the ππ* transition. Moreover, conformational changes induced by the cis↔ trans azopeptidomimetic switch were investigated by NMR in different solvents. |
topic |
azobenzene cis/trans photoisomerization photoswitchable peptide optical control NMR spectroscopy UV/Vis spectroscopy |
url |
https://www.frontiersin.org/article/10.3389/fchem.2019.00180/full |
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