Evidence map›Paper›PMID 34455461›Full record

ArticleEuropean biophysics journal : EBJ2021

Effective inhibition of insulin amyloid fibril aggregation by nickel(II) complexes containing heterocyclic thiosemicarbazones.

Kannayiram Gomathi, Jebiti Haribabu, Sivaraj Saranya, Dasararaju Gayathri, Kumaramangalam Jeyalakshmi, Subramanian Sendilvelan, Cesar Echeverria, Ramasamy Karvembu

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Article in European biophysics journal : EBJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.1field-weighted citation impact, top 19% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. 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

8 authors at 5 institutions in 3 countries.

Kannayiram Gomathi *Department of Mechanical Engineering, Dr. MGR Educational and Research Institute, Maduravoyal, Chennai, 600095, India. gomathi.ibt@drmgrdu.ac.in.ORCID http://orcid.org/0000-0002-6247-0070
Jebiti Haribabu *Department of Chemistry, National Institute of Technology, Tiruchirappalli, 620015, India.
Sivaraj SaranyaDepartment of Mechanical Engineering, Dr. MGR Educational and Research Institute, Maduravoyal, Chennai, 600095, India.
Dasararaju GayathriCentre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai, 600025, India.
Kumaramangalam JeyalakshmiDepartment of Chemistry, National Institute of Technology, Tiruchirappalli, 620015, India.
Subramanian SendilvelanDepartment of Mechanical Engineering, Dr. MGR Educational and Research Institute, Maduravoyal, Chennai, 600095, India.
Cesar EcheverriaFacultad de Medicina, Universidad de Atacama, Copayapu 485, 1531772, Copiapo, Chile.
Ramasamy KarvembuDepartment of Chemistry, National Institute of Technology, Tiruchirappalli, 620015, India. kar@nitt.edu.
National Institute of Technology Tiruchirappalli · INDr. M.G.R. Educational and Research Institute · INUniversity Health Network · CAUniversity of Atacama · CLUniversity of Madras · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The sensitivity of protein molecular structures makes them susceptible to aggregation in conditions unfavorable for the maintenance of their native folds. The aggregation of proteins leads to many disorders, but the inhibition of amyloid fibril formation using metal-containing small molecules is gaining popularity. Herein we report the effect of nickel(II) complexes (N1, N2, N3, and N4) bearing thiosemicarbazones on the inhibition of amyloid fibril formation by insulin. The interactions of the complexes with amyloid fibrils were investigated using various biophysical techniques, including light scattering, intrinsic fluorescence assay, thioflavin T (ThT) assay, and Fourier transform-infrared spectroscopy. The results revealed that the phenyl-substituted N3 was an efficient inhibitor of amyloid fibril formation and maintained the insulin in its native structure despite conditions promoting fibrillation. Nickel(II) complexes containing indole based thiosemicarbazones were efficient in inhibiting the amyloid fibril formation and maintaining the insulin in its native structure in unfavorable conditions.

Indexed as

AmyloidThiosemicarbazonesFluorescenceInsulinNickelAmyloidInsulinNickelThiosemicarbazonesInsulin aggregationMolecular dockingNi(II) complexesThiosemicarbazone

Identifiers

PMID34455461
OpenAlexW3196945862

What OpenQuestion holds

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Read underepoch 390

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.