Short hydrogen bonds enhance nonaromatic protein-related fluorescence
| Autor: | J. Axel Zeitler, Philippa J. Woodhams, Gabriele S. Kaminski Schierle, Gonzalo Diaz Miron, Amberley D. Stephens, Michael T. Ruggiero, Elyse M. Kleist, Uriel N. Morzan, Ali Hassanali, Luca Grisanti, Dan Credgington, Andrew D. Bond, Saul T. E. Jones, Muhammad Nawaz Qaisrani, Ralph Gebauer, Mariano C. González Lebrero, Emiliano Poli |
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| Přispěvatelé: | Stephens, Amberley D [0000-0002-7303-6392], Qaisrani, Muhammad Nawaz [0000-0003-4167-3116], Ruggiero, Michael T [0000-0003-1848-2565], Woodhams, Philippa J [0000-0003-4537-5976], Kleist, Elyse M [0000-0001-8596-659X], Zeitler, J Axel [0000-0002-4958-0582], Kaminski Schierle, Gabriele S [0000-0002-1843-2202], Apollo - University of Cambridge Repository |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Chemical transformation
Optics and Photonics Glutamine Intrinsic fluorescence Molecular Dynamics Simulation Photochemistry Fluorescence Ab initio molecular dynamics Ammonia Humans Single amino acid short hydrogen bond Density Functional Theory Multidisciplinary Hydrogen bond Chemistry intrinsic fluorescence ultraviolet fluorescence Hydrogen Bonding Conical intersection Biophysics and Computational Biology Excited state Physical Sciences Peptides |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | Significance Intrinsic fluorescence of nonaromatic amino acids is a puzzling phenomenon with an enormous potential in biophotonic applications. The physical origins of this effect, however, remain elusive. Herein, we demonstrate how specific hydrogen bond networks can modulate fluorescence. We highlight the key role played by short hydrogen bonds, present in the protein structure, on the ensuing fluorescence. We provide detailed experimental and molecular evidence to explain these unusual nonaromatic optical properties. Our findings should benefit the design of novel optically active biomaterials for applications in biosensing and imaging. Fluorescence in biological systems is usually associated with the presence of aromatic groups. Here, by employing a combined experimental and computational approach, we show that specific hydrogen bond networks can significantly affect fluorescence. In particular, we reveal that the single amino acid L-glutamine, by undergoing a chemical transformation leading to the formation of a short hydrogen bond, displays optical properties that are significantly enhanced compared with L-glutamine itself. Ab initio molecular dynamics simulations highlight that these short hydrogen bonds prevent the appearance of a conical intersection between the excited and the ground states and thereby significantly decrease nonradiative transition probabilities. Our findings open the door to the design of new photoactive materials with biophotonic applications. |
| Databáze: | OpenAIRE |
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