ArticleFrontiers in chemistry2019
A Photochromic Azobenzene Peptidomimetic of a β-Turn Model Peptide Structure as a Conformational Switch.
Article in Frontiers in chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Light-activated azobenzene peptide inhibitor of the PD-1/PD-L1 interaction.Chemical communications (Cambridge, England) · 2024Article
- Photocontrolled Reversible Amyloid Fibril Formation of Parathyroid Hormone-Derived Peptides.Bioconjugate chemistry · 2024Article
- Photocontrol of the β-Hairpin Polypeptide Structure through an Optimized Azobenzene-Based Amino Acid Analogue.Journal of the American Chemical Society · 2024Article
- Helicase Activity Modulation with On-Demand Light-Based Conformational Control.Journal of the American Chemical Society · 2023Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 [Pro
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