Evidence map›Paper›PMID 25189418›Full record

ArticleScientific reports2014

Tuning calcite morphology and growth acceleration by a rational design of highly stable protein-mimetics.

Chun-Long Chen, Jiahui Qi, Jinhui Tao, Ronald N Zuckermann, James J DeYoreo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
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  3. A molecular view of peptoid-induced acceleration of calcite growth.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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.

Chun-Long Chen1] Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 [2] Pacific Northwest National Laboratory, PO Box 999, MS K2-01, Richland, WA 99352.
Jiahui Qi1] Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 [2] Department of Materials, Imperial College London, London, SW7 2AZ.
Jinhui Tao1] Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 [2] Pacific Northwest National Laboratory, PO Box 999, MS K2-01, Richland, WA 99352.
Ronald N ZuckermannMolecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720.
James J DeYoreo1] Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 [2] Pacific Northwest National Laboratory, PO Box 999, MS K2-01, Richland, WA 99352 [3] Department of Materials Science and Engineering, University of Washington, Seattle, WA 98195.
Lawrence Berkeley National Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In nature, proteins play a significant role in biomineral formation. One of the ultimate goals of bioinspired materials science is to develop highly stable synthetic molecules that mimic the function of these natural proteins by controlling crystal formation. Here, we demonstrate that both the morphology and the degree of acceleration or inhibition observed during growth of calcite in the presence of peptoids can be rationally tuned by balancing the electrostatic and hydrophobic interactions, with hydrophobic interactions playing the dominant role. While either strong electrostatic or hydrophobic interactions inhibit growth and reduces expression of the {104} faces, correlations between peptoid-crystal binding energies and observed changes in calcite growth indicate moderate electrostatic interactions allow peptoids to weakly adsorb while moderate hydrophobic interactions cause disruption of surface-adsorbed water layers, leading to growth acceleration with retained expression of the {104} faces. This study provides fundamental principles for designing peptoids as crystallization promoters, and offers a straightforward screening method based on macroscopic crystal morphology. Because peptoids are sequence-specific, highly stable, and easily synthesized, peptoid-enhanced crystallization offers a broad range of potential applications.

Indexed as

Calcium CarbonateCarboxylic AcidsCrystallizationHydrophobic and Hydrophilic InteractionsMolecular MimicryPeptoidsCalcium CarbonateCarboxylic AcidsPeptoids

Identifiers

PMID25189418
PMCPMC5385837
OpenAlexW1991221075

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.