Evidence map›Paper›PMID 32759766›Full record

ArticleMolecules (Basel, Switzerland)2020

Far-Off Resonance: Multiwavelength Raman Spectroscopy Probing Amide Bands of Amyloid-β-(37-42) Peptide.

Martynas Talaikis, Simona Strazdaitė, Mantas Žiaunys, Gediminas Niaura

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Raman signatures ofFrontiers in microbiology · 2026
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  8. Direct observation of the effects of chemical fixation in MNT-1 cells: A SE-ADM and Raman study.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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

4 authors at 2 institutions in 1 country.

Martynas TalaikisDepartment of Bioelectrochemistry and Biospectroscopy, Institute of Biochemistry, Life Sciences Center, Vilnius University, Saulėtekis Ave. 7, LT-10257 Vilnius, Lithuania.ORCID 0000-0003-3516-6425
Simona StrazdaitėDepartment of Organic Chemistry, Center for Physical Sciences and Technology (FTMC), Saulėtekis Ave. 3, LT-10257 Vilnius, Lithuania.ORCID 0000-0003-0007-5507
Mantas ŽiaunysInstitute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekis Ave. 7, LT-10257 Vilnius, Lithuania.
Gediminas NiauraDepartment of Organic Chemistry, Center for Physical Sciences and Technology (FTMC), Saulėtekis Ave. 3, LT-10257 Vilnius, Lithuania.
Center for Physical Sciences and Technology · LTVilnius University · LT

Funding

H2020 Marie Skłodowska-Curie Actions 792508
6 · The paper itself

Abstract

Several neurodegenerative diseases, like Alzheimer's and Parkinson's are linked with protein aggregation into amyloid fibrils. Conformational changes of native protein into the β-sheet structure are associated with a significant change in the vibrational spectrum. This is especially true for amide bands which are inherently sensitive to the secondary structure of a protein. Raman amide bands are greatly intensified under resonance conditions, in the UV spectral range, allowing for the selective probing of the peptide backbone. In this work, we examine parallel β-sheet forming GGVVIA, the C-terminus segment of amyloid-β peptide, using UV-Vis, FTIR, and multiwavelength Raman spectroscopy. We find that amide bands are enhanced far from the expected UV range, i.e., at 442 nm. A reasonable two-fold relative intensity increase is observed for amide II mode (normalized according to the δCH

Indexed as

AmidesAmino Acid SequenceAmyloidAmyloid beta-PeptidesHumansMicroscopy, Atomic ForceMolecular StructureProtein AggregatesProtein Aggregation, PathologicalProtein Structure, SecondarySpectrum Analysis, RamanAmidesAmyloidAmyloid beta-PeptidesProtein Aggregatesamide IIamyloid fibrilprotein aggregationRaman spectroscopysecondary structureβ-sheet

Identifiers

PMID32759766
PMCPMC7435454
OpenAlexW3047483808

What OpenQuestion holds

Textmetadata
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.