Evidence map›Paper›PMID 37010879›Full record

ArticleACS applied materials & interfaces2023

Insight into the Binding Mechanisms of Quartz-Selective Peptides: Toward Greener Flotation Processes.

Abolfazl Alizadeh Sahraei, Barbara Mejia Bohorquez, Denise Tremblay, Sylvain Moineau, Alain Garnier, Faïçal Larachi, Patrick Lagüe

Abstract read
In one paragraph

Article in ACS applied materials & interfaces, 2023. 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
–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

3 citing papers in PubMed.

  1. Article
  2. Review
  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

7 authors.

Abolfazl Alizadeh SahraeiDepartment of Chemical Engineering, Université Laval, 1065 Avenue de la Médecine, Québec, Québec G1V 0A6, Canada.ORCID 0000-0001-7103-7001
Barbara Mejia BohorquezDepartment of Chemical Engineering, Université Laval, 1065 Avenue de la Médecine, Québec, Québec G1V 0A6, Canada.
Denise TremblayPROTEO, The Quebec Network for Research on Protein Function, Engineering, and Applications, 1045 Avenue de la Médecine, Québec, Québec G1V 0A6, Canada.
Sylvain MoineauPROTEO, The Quebec Network for Research on Protein Function, Engineering, and Applications, 1045 Avenue de la Médecine, Québec, Québec G1V 0A6, Canada.ORCID 0000-0002-2832-5101
Alain GarnierDepartment of Chemical Engineering, Université Laval, 1065 Avenue de la Médecine, Québec, Québec G1V 0A6, Canada.
Faïçal LarachiDepartment of Chemical Engineering, Université Laval, 1065 Avenue de la Médecine, Québec, Québec G1V 0A6, Canada.ORCID 0000-0002-0127-4738
Patrick LagüePROTEO, The Quebec Network for Research on Protein Function, Engineering, and Applications, 1045 Avenue de la Médecine, Québec, Québec G1V 0A6, Canada.ORCID 0000-0002-5236-4979

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mining practices, chiefly froth flotation, are being critically reassessed to replace their use of biohazardous chemical reagents in favor of biofriendly alternatives as a path toward green processes. In this regard, this study aimed at evaluating the interactions of peptides, as potential floatation collectors, with quartz using phage display and molecular dynamics (MD) simulations. Quartz-selective peptide sequences were initially identified by phage display at pH = 9 and further modeled by a robust simulation scheme combining classical MD, replica exchange MD, and steered MD calculations. Our residue-specific analyses of the peptides revealed that positively charged arginine and lysine residues were favorably attracted by the quartz surface at basic pH. The negatively charged residues at pH 9 (i.e., aspartic acid and glutamic acid) further showed affinity toward the quartz surface through electrostatic interactions with the positively charged surface-bound Na

Indexed as

PeptidesQuartzAdsorptionAmino Acid SequenceMineralsMolecular Dynamics SimulationMineralsPeptidesQuartzfloatationmolecular dynamicspeptidesphage displayquartzrational designREMDSMD

Identifiers

PMID37010879
PMCPMC10103053

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.