Evidence map›Paper›PMID 33673072›Full record

ArticleMolecules (Basel, Switzerland)2021

On the Protein Fibrillation Pathway: Oligomer Intermediates Detection Using ATR-FTIR Spectroscopy.

Jelica Milošević, Radivoje Prodanović, Natalija Polović

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
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  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation.International journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein ofInternational journal of molecular sciences · 2021
    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

3 authors.

Jelica MiloševićDepartment of Biochemistry, Faculty of Chemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia.
Radivoje ProdanovićDepartment of Biochemistry, Faculty of Chemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia.ORCID 0000-0003-4662-1825
Natalija PolovićDepartment of Biochemistry, Faculty of Chemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia.ORCID 0000-0002-9127-2014

Funding

Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja 451-03-68/2020-14/200168
6 · The paper itself

Abstract

Oligomeric intermediates on the pathway of amyloid fibrillation are suspected as the main cytotoxins responsible for amyloid-related pathogenicity. As they appear to be a part of the lag phase of amyloid fibrillation when analyzed using standard methods such as Thioflavin T (ThT) fluorescence, a more sensitive method is needed for their detection. Here we apply Fourier transform infrared spectroscopy (FTIR) in attenuated total reflectance (ATR) mode for fast and cheap analysis of destabilized hen-egg-white lysozyme solution and detection of oligomer intermediates of amyloid fibrillation. Standard methods of protein aggregation analysis- Thioflavin T (ThT) fluorescence, atomic force microscopy (AFM), and 8-anilinonaphthalene-1-sulphonic acid (ANS) fluorescence were applied and compared to FTIR spectroscopy data. Results show the great potential of FTIR for both, qualitative and quantitative monitoring of oligomer formation based on the secondary structure changes. While oligomer intermediates do not induce significant changes in ThT fluorescence, their secondary structure changes were very prominent. Normalization of specific Amide I region peak intensities by using Amide II peak intensity as an internal standard provides an opportunity to use FTIR spectroscopy for both qualitative and quantitative analysis of biological samples and detection of potentially toxic oligomers, as well as for screening of efficiency of fibrillation procedures.

Indexed as

AmyloidAmyloidogenic ProteinsAnimalsBenzothiazolesChickensFluorescenceMicroscopy, Atomic ForceMuramidaseProtein Structure, SecondarySpectroscopy, Fourier Transform InfraredAmyloidAmyloidogenic ProteinsBenzothiazoleshen egg lysozymeMuramidasethioflavin Tamyloid fibrillationATR FTIRHEWLoligomer intermediatessecondary structure perturbation

Identifiers

PMID33673072
PMCPMC7918411

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Registered trials

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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.