Evidence map›Paper›PMID 28542206›Full record

ArticlePloS one2017

Carbonyl-based blue autofluorescence of proteins and amino acids.

Chamani Niyangoda, Tatiana Miti, Leonid Breydo, Vladimir Uversky, Martin Muschol

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.5field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Article
  3. Anomalous Water Fluorescence Induced by Solutes.The journal of physical chemistry letters · 2025
    Article
  4. Crystallization of L-Cysteine in Heavy Water Induces Intrinsic Fluorescence.Angewandte Chemie (International ed. in English) · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Amyloid Fibrils of Stefin B Show Anisotropic Properties.International journal of molecular sciences · 2023
    Article
  12. Article
  13. One- and Two-Photon Excited Autofluorescence of Lysozyme Amyloids.The journal of physical chemistry letters · 2022
    Article
  14. Article
  15. Fluorescence Emission of Self-assembling Amyloid-like Peptides: Solution versus Solid State.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  16. Article
  17. Short hydrogen bonds enhance nonaromatic protein-related fluorescence.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Chamani NiyangodaDepartment of Physics, University of South Florida, Tampa, Florida, United States of America.
Tatiana MitiDepartment of Physics, University of South Florida, Tampa, Florida, United States of America.
Leonid BreydoDepartment of Molecular Medicine, USF Health, Tampa, Florida, United States of America.
Vladimir UverskyDepartment of Molecular Medicine, USF Health, Tampa, Florida, United States of America.
Martin MuscholDepartment of Physics, University of South Florida, Tampa, Florida, United States of America.ORCID http://orcid.org/0000-0002-6488-0049
University of South Florida · US

Funding

Does Charge Repulsion of Amyloids Regulate their Assembly Pathways and Toxicity?R15GM097723 · NIGMS · UNIVERSITY OF SOUTH FLORIDA · PI MUSCHOL, MARTIN · 2012 to 2016
$773k
NIGMS NIH HHS R15 GM097723
6 · The paper itself

Abstract

Intrinsic protein fluorescence is inextricably linked to the near-UV autofluorescence of aromatic amino acids. Here we show that a novel deep-blue autofluorescence (dbAF), previously thought to emerge as a result of protein aggregation, is present at the level of monomeric proteins and even poly- and single amino acids. Just as its aggregation-related counterpart, this autofluorescence does not depend on aromatic residues, can be excited at the long wavelength edge of the UV and emits in the deep blue. Differences in dbAF excitation and emission peaks and intensities from proteins and single amino acids upon changes in solution conditions suggest dbAF's sensitivity to both the chemical identity and solution environment of amino acids. Autofluorescence comparable to dbAF is emitted by carbonyl-containing organic solvents, but not those lacking the carbonyl group. This implicates the carbonyl double bonds as the likely source for the autofluorescence in all these compounds. Using beta-lactoglobulin and proline, we have measured the molar extinction coefficients and quantum yields for dbAF in the monomeric state. To establish its potential utility in monitoring protein biophysics, we show that dbAF emission undergoes a red-shift comparable in magnitude to tryptophan upon thermal denaturation of lysozyme, and that it is sensitive to quenching by acrylamide. Carbonyl dbAF therefore provides a previously neglected intrinsic optical probe for investigating the structure and dynamics of amino acids, proteins and, by extension, DNA and RNA.

Indexed as

AcrylamideAmino AcidsFluorescenceLactoglobulinsOptical ImagingProlineProteinsSolutionsSpectrometry, FluorescenceTryptophanAcrylamideAmino AcidsLactoglobulinsProlineProteinsSolutionsTryptophan

Identifiers

PMID28542206
PMCPMC5444599
OpenAlexW2619593685

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.