On the purported 'backbone fluorescence' in protein three-dimensional fluorescence spectra
| Autor: | Marco van de Weert, Sara Bobone, Saad Tayyab, Noor Hafizan B. Bahring, Annalisa Bortolotti, Lorenzo Stella, Yin How Wong, Stine S. Korsholm |
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| Rok vydání: | 2016 |
| Předmět: |
Stereochemistry
General Chemical Engineering 02 engineering and technology 010402 general chemistry Photochemistry 01 natural sciences Spectral line chemistry.chemical_compound Side chain Aromatic amino acids Peptide bond Proteins fluorescence Tryptophan Tyrosine Peptides Emission spectrum Settore CHIM/02 - Chimica Fisica Chemistry Tryptophan General Chemistry 021001 nanoscience & nanotechnology Fluorescence 0104 chemical sciences Excited state fluorescence 0210 nano-technology Excitation |
| Zdroj: | Bortolotti, A, Wong, Y H, Korsholm, S S, Bahring, N H B, Bobone, S, Tayyab, S, Van De Weert, M & Stella, L 2016, ' On the purported "backbone fluorescence" in protein three-dimensional fluorescence spectra ', RSC Advances, vol. 6, no. 114, pp. 112870-112876 . https://doi.org/10.1039/c6ra23426g |
| ISSN: | 2046-2069 |
| DOI: | 10.1039/c6ra23426g |
| Popis: | In this study, several proteins (albumin, lysozyme, insulin) and model compounds (Trp, Tyr, homopolypeptides) were used to demonstrate the origin of the fluorescence observed upon their excitation at 220-230 nm. In the last 10 years we have observed a worrying increase in the number of articles claiming that this fluorescence originates from the protein backbone, contrary to the established knowledge that UV protein emission is due to aromatic amino acids only. Overall, our data clearly demonstrate that the observed emission upon excitation at 220-230 nm is due to the excitation of Tyr and/or Trp, with subsequent emission from the lowest excited state (i.e. the same as obtained with 280 nm excitation) in agreement with Kasha's rule. Therefore, this fluorescence peak does not provide any information on backbone conformation, but simply reports on the local environment around the aromatic side chains, just as any traditional protein emission spectrum. The many papers in reputable journals erroneously reporting this peak assignment, contradicting 5 decades of prior knowledge, have led to the creation of a new dogma, where many authors and reviewers now take the purported backbone fluorescence as an established fact. We hope the current paper helps counter this new situation and leads to a reassessment of those papers that make this erroneous claim. |
| Databáze: | OpenAIRE |
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