Evidence map›Paper›PMID 34458846›Full record

ArticleMaterials advances2021

Gallium nanoparticles as novel inhibitors of Aβ40 aggregation.

Kyabeth M Torres, Ambar S Delgado, Erika R Serrano, Nitza V Falcón-Cruz, Anamaris Meléndez, Idalia Ramos, Deguo Du, Rolando Oyola

Open access · goldAbstract read
In one paragraph

Article in Materials advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 56% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 institutions in 2 countries.

Kyabeth M TorresUniversity of Puerto Rico-Humacao, Department of Biology, Call Box 860 Humacao 00792 PR USA.
Ambar S DelgadoUniversity of Puerto Rico-Humacao, Department of Biology, Call Box 860 Humacao 00792 PR USA.
Erika R SerranoUniversity of Puerto Rico-Humacao, Department of Chemistry, Call Box 860 Humacao 00792 PR USA rolando.oyola@upr.edu.
Nitza V Falcón-CruzUniversity of Puerto Rico-Humacao, Department of Chemistry, Call Box 860 Humacao 00792 PR USA rolando.oyola@upr.edu.
Anamaris MeléndezUniversity of Puerto Rico-Humacao, Department of Physics & Electronics, Call Box 860 Humacao 00792 PR USA.
Idalia RamosUniversity of Puerto Rico-Humacao, Department of Physics & Electronics, Call Box 860 Humacao 00792 PR USA.ORCID https://orcid.org/0000-0001-7467-4209
Deguo DuFlorida Atlantic University, Department of Chemistry & Biochemistry Boca Raton 33431 FL USA ddu@fau.edu.ORCID https://orcid.org/0000-0002-8701-8208
Rolando OyolaUniversity of Puerto Rico-Humacao, Department of Chemistry, Call Box 860 Humacao 00792 PR USA rolando.oyola@upr.edu.ORCID https://orcid.org/0000-0003-0258-4620
University of Puerto Rico at Humacao · PRFlorida Atlantic University · US

Funding

UPR-Humacao Maximizing Access to Research Careers Undergraduate Student Training in Academic Research ProgramT34GM008156 · NIGMS · UNIVERSITY OF PUERTO RICO AT HUMACAO · PI TRAVERSO, EDWIN E, VEGA-BERMUDEZ, ESTHER Z · 1986 to 2021
$5.4M
Role of the N-terminal Region in Abeta Oligomer and Fibril FormationR15GM116006 · NIGMS · FLORIDA ATLANTIC UNIVERSITY · PI DU, DEGUO · 2015 to 2020
$735k
NIGMS NIH HHS R15 GM116006NIGMS NIH HHS T34 GM008156
6 · The paper itself

Abstract

Alzheimer's disease (AD) has been consistently related to the formation of senile amyloid plaques mainly composed of amyloid β (Aβ) peptides. The toxicity of Aβ aggregates has been indicated to be responsible for AD pathology. One scenario to decrease Aβ toxicity is the development of effective inhibitors against Aβ amyloid formation. In this study, we investigate the effect of gallium nitride nanoparticles (GaN NPs) as inhibitors of Aβ40 amyloid formation using a combination of biophysical approaches. Our results show that the lag phase of Aβ40 aggregation kinetics is significantly retarded by GaN NPs in a concentration dependent manner, implying the activity of GaN NPs in interfering with the formation of the crucial nucleus during Aβ aggregation. Our results also show that GaN NPs can reduce the amyloid fibril elongation rate in the course of the aggregation kinetics. It is speculated that the high polarization characteristics of GaN NPs may provoke a strong interaction between the particles and Aβ40 peptide and in this way decrease self-association of the peptide monomers to form amyloids.

Identifiers

PMID34458846
PMCPMC8366391
OpenAlexW3179792893

What OpenQuestion holds

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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.