Evidence map›Paper›PMID 41603486›Full record

ReviewChemistry, an Asian journal2026

Advances in Synchrotron Radiation-Based Vacuum-Ultraviolet Circular Dichroism for Biomolecular Structural Analysis.

Koichi Matsuo, Satoshi Hashimoto, Ryota Imaura, Mohamed I A Ibrahim

Abstract readReview
In one paragraph

Review in Chemistry, an Asian journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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.

Koichi MatsuoResearch Institute for Synchrotron Radiation Science (HiSOR), Hiroshima University, Higashi-Hiroshima, Japan.ORCID 0000-0001-8166-544X
Satoshi HashimotoResearch Institute for Synchrotron Radiation Science (HiSOR), Hiroshima University, Higashi-Hiroshima, Japan.
Ryota ImauraGraduate School of Advanced Science and Engineering, Hiroshima University, Higashi-Hiroshima, Japan.
Mohamed I A IbrahimResearch Institute for Synchrotron Radiation Science (HiSOR), Hiroshima University, Higashi-Hiroshima, Japan.

Funding

Grants-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan 22K06163Grants-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan 23H04597Grants-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan 25H01630Satake Technology Foundation
6 · The paper itself

Abstract

Vacuum-ultraviolet circular dichroism (VUVCD) spectroscopy using synchrotron radiation is a powerful tool for characterizing the structures of biomolecules in aqueous solutions. When combined with bioinformatics, VUVCD enables detailed determination of protein secondary-structure contents, segment numbers, and sequence distributions, while coupling with linear dichroism and shear flow techniques provides insights into the orientations of secondary structures. These analytical approaches have been applied to the structural characterization of membrane-bound α-synuclein (αS), a protein which transforms into amyloid fibrils associated with Parkinson's disease, successfully revealing the molecular mechanism of αS fibril-formation on membranes. Furthermore, time-resolved measurements using microfluidic device allow direct observation of protein structural dynamics during membrane interactions. The combination of VUVCD spectroscopy with molecular dynamics simulations in aqueous environments has also been applied to determine the absolute configurations of saccharides containing higher-energy chromophores, thereby elucidating hydration structures involving intra- and intermolecular hydrogen bonds. Recent studies have further expanded these applications to monitor the conformational changes of extracellular polysaccharides and polyhydroxyalkanoates as functions of temperature and membrane interactions. These advancements highlight that integrating VUVCD spectroscopy with computational and other experimental approaches can significantly enhance the structural characterization of diverse biomolecules at molecular level.

Indexed as

alpha-SynucleinCircular DichroismSynchrotronsHumansMolecular Dynamics SimulationProtein Structure, SecondaryUltraviolet RaysVacuumalpha-Synucleinbiopolymersproteinssaccharidessynchrotron radiationvacuum‐ultraviolet circular dichroism

Identifiers

PMID41603486
PMCPMC12849548

What OpenQuestion holds

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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.