Evidence map›Paper›PMID 37640827›Full record

ArticleAnalytical and bioanalytical chemistry2023

Investigating biochemical and structural changes of glycated collagen using multimodal multiphoton imaging, Raman spectroscopy, and atomic force microscopy.

Elsie Quansah, Tanveer Ahmed Shaik, Ecehan Çevik, Xinyue Wang, Christiane Höppener, Tobias Meyer-Zedler, Volker Deckert, Michael Schmitt, Jürgen Popp, Christoph Krafft

Open access · hybridAbstract read
In one paragraph

Article in Analytical and bioanalytical chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. 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

10 authors at 2 institutions in 1 country.

Elsie QuansahInstitute of Physical Chemistry and Abbe Center of Photonics (IPC), Member of the Leibniz Center for Photonics in Infectious Research (LPI), Friedrich Schiller University Jena, Helmholtzweg 4, 07743, Jena, Germany.
Tanveer Ahmed ShaikLeibniz Institute of Photonic Technology (IPHT), Member of Leibniz Health Technologies, Member of the Leibniz Center for Photonics in Infectious Research (LPI), Albert-Einstein-Straße 9, 07745, Jena, Germany.
Ecehan ÇevikLeibniz Institute of Photonic Technology (IPHT), Member of Leibniz Health Technologies, Member of the Leibniz Center for Photonics in Infectious Research (LPI), Albert-Einstein-Straße 9, 07745, Jena, Germany.
Xinyue WangInstitute of Physical Chemistry and Abbe Center of Photonics (IPC), Member of the Leibniz Center for Photonics in Infectious Research (LPI), Friedrich Schiller University Jena, Helmholtzweg 4, 07743, Jena, Germany.
Christiane HöppenerInstitute of Physical Chemistry and Abbe Center of Photonics (IPC), Member of the Leibniz Center for Photonics in Infectious Research (LPI), Friedrich Schiller University Jena, Helmholtzweg 4, 07743, Jena, Germany.
Tobias Meyer-ZedlerInstitute of Physical Chemistry and Abbe Center of Photonics (IPC), Member of the Leibniz Center for Photonics in Infectious Research (LPI), Friedrich Schiller University Jena, Helmholtzweg 4, 07743, Jena, Germany.
Volker DeckertInstitute of Physical Chemistry and Abbe Center of Photonics (IPC), Member of the Leibniz Center for Photonics in Infectious Research (LPI), Friedrich Schiller University Jena, Helmholtzweg 4, 07743, Jena, Germany.
Michael SchmittInstitute of Physical Chemistry and Abbe Center of Photonics (IPC), Member of the Leibniz Center for Photonics in Infectious Research (LPI), Friedrich Schiller University Jena, Helmholtzweg 4, 07743, Jena, Germany.
Jürgen PoppInstitute of Physical Chemistry and Abbe Center of Photonics (IPC), Member of the Leibniz Center for Photonics in Infectious Research (LPI), Friedrich Schiller University Jena, Helmholtzweg 4, 07743, Jena, Germany.
Christoph KrafftLeibniz Institute of Photonic Technology (IPHT), Member of Leibniz Health Technologies, Member of the Leibniz Center for Photonics in Infectious Research (LPI), Albert-Einstein-Straße 9, 07745, Jena, Germany. Christoph.krafft@leibniz-ipht.de.
Leibniz Institute of Photonic Technology · DEFriedrich Schiller University Jena · DE

Funding

Deutsche Forschungsgemeinschaft Polytarget / CRC/SFB-1278Deutsche Forschungsgemeinschaft Project B04Freistaat Thüringen ThIMEDOP / FKZ IZN 2018 0002
6 · The paper itself

Abstract

Advanced glycation end products (AGEs) form extracellular crosslinking with collagenous proteins, which contributes to the development of diabetic complications. In this study, AGEs-related pentosidine (PENT) crosslinks-induced structural and biochemical changes are studied using multimodal multiphoton imaging, Raman spectroscopy and atomic force microscopy (AFM). Decellularized equine pericardium (EP) was glycated with four ribose concentrations ranging between 5 and 200 mM and monitored for up to 30 days. Two-photon excited fluorescence (TPEF) and second harmonic generation (SHG) microscopic imaging probed elastin and collagen fibers, respectively. The glycated EP showed a decrease in the SHG intensities associated with loss of non-centrosymmetry of collagen and an increase of TPEF intensities associated with PENT crosslinks upon glycation. TPEF signals from elastin fibers were unaffected. A three-dimensional reconstruction with SHG + TPEF z-stack images visualized the distribution of collagen and elastin within the EP volume matrix. In addition, Raman spectroscopy (RS) detected changes in collagen-related bands and discriminated glycated from untreated EP. Furthermore, AFM scans showed that the roughness increases and the D-unit structure of fibers remained unchanged during glycation. The PENT crosslinked-induced changes are discussed in the context of previous studies of glutaraldehyde- and genipin-induced crosslinking and collagenase-induced digestion of collagen. We conclude that TPEF, SHG, RS, and AFM are effective, label-free, and non-destructive methods to investigate glycated tissues, differentiate crosslinking processes, and characterize general collagen-associated and disease-related changes, in particular by their RS fingerprints.

Indexed as

CollagenMicroscopy, Atomic ForceMicroscopy, Fluorescence, MultiphotonSpectrum Analysis, RamanAnimalsElastinGlycation End Products, AdvancedGlycosylationHorsesCollagenElastinGlycation End Products, AdvancedAdvanced glycation end productsAtomic force microscopyCollagen crosslinkingRaman spectroscopySecond harmonic generationTwo-photon excited fluorescence

Identifiers

PMID37640827
PMCPMC10558391
OpenAlexW4386210582

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.