Evidence map›Paper›PMID 36500427›Full record

ArticleMolecules (Basel, Switzerland)2022

Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid.

Cynthia Regina Albrecht Mahl, Rogério Aparecido Bataglioli, Guilherme Bedeschi Calais, Thiago Bezerra Taketa, Marisa Masumi Beppu

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

5 authors at 1 institution in 1 country.

Cynthia Regina Albrecht MahlSchool of Chemical Engineering, University of Campinas, UNICAMP, 500 Albert Einstein Av., Campinas 13083-852, SP, Brazil.
Rogério Aparecido BataglioliSchool of Chemical Engineering, University of Campinas, UNICAMP, 500 Albert Einstein Av., Campinas 13083-852, SP, Brazil.
Guilherme Bedeschi CalaisSchool of Chemical Engineering, University of Campinas, UNICAMP, 500 Albert Einstein Av., Campinas 13083-852, SP, Brazil.ORCID 0000-0003-4222-1437
Thiago Bezerra TaketaSchool of Chemical Engineering, University of Campinas, UNICAMP, 500 Albert Einstein Av., Campinas 13083-852, SP, Brazil.
Marisa Masumi BeppuSchool of Chemical Engineering, University of Campinas, UNICAMP, 500 Albert Einstein Av., Campinas 13083-852, SP, Brazil.
Universidade Estadual de Campinas (UNICAMP) · BR

Funding

Coordenação de Aperfeicoamento de Pessoal de Nível Superior 88882.151600/2017-01Coordenação de Aperfeicoamento de Pessoal de Nível Superior 88887.513482/2020-00
6 · The paper itself

Abstract

The anomalous interaction between metal ions and the peptide beta-amyloid is one of the hallmarks of Alzheimer's disease. Metal-binding biopolymers, including polysaccharides, can elucidate the fundamental aspects of metal ions' interactions with biological tissue and their interplay in Alzheimer's disease. This work focuses on the role of the alginate composition on Cu(II) adsorption in the presence of histidine or β-amyloid, the peptide associated with the progression of Alzheimer's disease. Alginate samples with different mannuronic/guluronic (M/G) ratios led to similar Cu(II) adsorption capacities, following the Langmuir isotherm and the pseudo-second-order adsorption kinetic models. Although the presence of histidine produced up to a 20% reduction in the copper adsorption capacity in guluronic-rich alginate samples (M/G~0.61), they presented stable bidentate chelation of the metallic ion. Chemical analyses (FTIR and XPS) demonstrated the role of hydroxyl and carboxyl groups in copper ion chelation, whereas both crystallinity and morphology analyses indicated the prevalence of histidine interaction with guluronic-rich alginate. Similar results were observed for Cu(II) adsorption in alginate beads in the presence of beta-amyloid and histidine, suggesting that the alginate/histidine system is a simple yet representative model to probe the application of biopolymers to metal ion uptake in the presence of biological competitors.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAdsorptionAlginatesBiopolymersCopperHistidineHumansHydrogen-Ion ConcentrationIonsKineticsAlginatesAmyloid beta-PeptidesBiopolymersCopperHistidineIonsalginateAlzheimer’s diseasebeta-amyloidcopper adsorptionhistidine

Identifiers

PMID36500427
PMCPMC9735935
OpenAlexW4310382675

What OpenQuestion holds

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LicenceCC BY
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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.