Evidence map›Paper›PMID 26041015›Full record

ArticleScientific reports2015

Surface Curvature Relation to Protein Adsorption for Carbon-based Nanomaterials.

Zonglin Gu, Zaixing Yang, Yu Chong, Cuicui Ge, Jeffrey K Weber, David R Bell, Ruhong Zhou

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

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  11. Fabrication and Functionalisation of Nanocarbon-Based Field-Effect Transistor Biosensors.Chembiochem : a European journal of chemical biology · 2022
    Review
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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

7 authors.

Zonglin GuInstitute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
Zaixing YangInstitute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
Yu ChongInstitute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
Cuicui GeInstitute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China.
Jeffrey K WeberIBM Thomas J. Watson Research Center, Yorktown Heights, NY 10598, USA.
David R BellIBM Thomas J. Watson Research Center, Yorktown Heights, NY 10598, USA.
Ruhong Zhou1] Institute of Quantitative Biology and Medicine, SRMP and RAD-X, Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou 215123, China [2] IBM Thomas J. Watson Research Center, Yorktown Heights, NY 10598, USA [3] Department of Chemistry, Columbia University, New York, NY 10027, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The adsorption of proteins onto carbon-based nanomaterials (CBNs) is dictated by hydrophobic and π-π interactions between aliphatic and aromatic residues and the conjugated CBN surface. Accordingly, protein adsorption is highly sensitive to topological constraints imposed by CBN surface structure; in particular, adsorption capacity is thought to increase as the incident surface curvature decreases. In this work, we couple Molecular Dynamics (MD) simulations with fluorescence spectroscopy experiments to characterize this curvature dependence in detail for the model protein bovine serum albumin (BSA). By studying BSA adsorption onto carbon nanotubes of increasing radius (featuring descending local curvatures) and a flat graphene sheet, we confirm that adsorption capacity is indeed enhanced on flatter surfaces. Naïve fluorescence experiments featuring multi-walled carbon nanotubes (MWCNTs), however, conform to an opposing trend. To reconcile these observations, we conduct additional MD simulations with MWCNTs that match those prepared in experiments; such simulations indicate that increased mass to surface area ratios in multi-walled systems explain the observed discrepancies. In reduction, our work substantiates the inverse relationship between protein adsorption capacity and surface curvature and further demonstrates the need for subtle consideration in experimental and simulation design.

Indexed as

Surface PropertiesAdsorptionAnimalsCarbonModels, MolecularNanostructuresProtein ConformationProteinsReproducibility of ResultsSerum Albumin, BovineSpectrometry, FluorescenceCarbonProteinsSerum Albumin, Bovine

Identifiers

PMID26041015
PMCPMC4455116

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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.