Evidence map›Paper›PMID 24156567›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2013

Potential-assisted adsorption of bovine serum albumin onto optically transparent carbon electrodes.

Tomás E Benavidez, Carlos D Garcia

Abstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

8 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Dielectric Spectroscopy Can Predict the Effect of External AC Fields on the Dynamic Adsorption of Lysozyme.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  3. Article
  4. Article
  5. Review
  6. Article
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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

2 authors at 1 institution in 1 country.

Tomás E BenavidezDepartment of Chemistry, The University of Texas at San Antonio , One UTSA Circle, San Antonio, Texas 78249, United States.
Carlos D Garcia
The University of Texas at San Antonio · US

Funding

RCMI Center for Interdiscplinary Health Research CIHRG12MD007591 · NIMHD · UNIVERSITY OF TEXAS SAN ANTONIO · PI PERRY, GEORGE · 2012 to 2016
$10.4M
UNDERSTANDING THE INTERACTION OF ANKYRINS AND NANOMATERIALSSC3GM081085 · NIGMS · UNIVERSITY OF TEXAS SAN ANTONIO · PI GARCIA, CARLOS DIEGO · 2007 to 2015
$844k
NIGMS NIH HHS 2SC3GM081085NIGMS NIH HHS SC3 GM081085NIMHD NIH HHS G12 MD007591NIMHD NIH HHS G12MD007591
6 · The paper itself

Abstract

This article describes the effect of the applied potential on the adsorption of bovine serum albumin (BSA) to optically transparent carbon electrodes (OTCE). To decouple the effect of the applied potential from the high affinity of the protein for the bare surface, the surface of the OTCE was initially saturated with a layer of BSA. Experiments described in the article show that potential values higher than +500 mV induced a secondary adsorption process (not observed at open-circuit potential), yielding significant changes in the thickness (and adsorbed amount) of the BSA layer obtained. Although the process showed a significant dependence on the experimental conditions selected, the application of higher potentials, selection of pH values around the isoelectric point (IEP) of the protein, high concentrations of protein, and low ionic strengths yielded faster kinetics and the accumulation of larger amounts of protein on the substrate. These experiments, obtained around the IEP of the protein, contrast with the traditional hypothesis that enhanced electrostatic interactions between the polarized substrate and the (oppositely charged) protein are solely responsible for the enhanced adsorption. These results suggest that the potential applied to the electrode is able to polarize the adsorbed layer and induce dipole-dipole interactions between the adsorbed and the incoming protein. This mechanism could be responsible for the potential-dependent oversaturation of the surface and could bolster to the development of surfaces with enhanced catalytic activity and implants with improved biocompatibility.

Indexed as

Optical PhenomenaAdsorptionAnimalsCarbonCattleElectrochemistryElectrodesHydrogen-Ion ConcentrationOsmolar ConcentrationSerum Albumin, BovineCarbonSerum Albumin, Bovine

Identifiers

PMID24156567
PMCPMC3867293
OpenAlexW2054313279

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.