Evidence map›Paper›PMID 25453976›Full record

ArticleBiomaterials2015

Combining an optical resonance biosensor with enzyme activity kinetics to understand protein adsorption and denaturation.

Kerry A Wilson, Craig A Finch, Phillip Anderson, Frank Vollmer, James J Hickman

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomaterials, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

5 citing papers in PubMed, 32 citations in OpenAlex.

  1. Developing choline oxidase immobilization on CoBioprocess and biosystems engineering · 2025
    Article
  2. Article
  3. Article
  4. Whispering gallery mode sensors.Advances in optics and photonics · 2015
    Article
  5. 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 2 institutions in 1 country.

Kerry A WilsonNanoscience Technology Center, University of Central Florida, 12424 Research Parkway, Orlando, FL 32826, USA.
Craig A FinchNanoscience Technology Center, University of Central Florida, 12424 Research Parkway, Orlando, FL 32826, USA.
Phillip AndersonNanoscience Technology Center, University of Central Florida, 12424 Research Parkway, Orlando, FL 32826, USA.
Frank VollmerThe Wyss & Rowland Institutes, Harvard University, 100 Edwin H. Land Blvd, Cambridge, MA 02142, USA.
James J HickmanNanoscience Technology Center, University of Central Florida, 12424 Research Parkway, Orlando, FL 32826, USA. Electronic address: jhickman@mail.ucf.edu.
University of Central Florida · USHarvard University · US

Funding

An In Vitro Model of Stem Cell Innervation of MyotubesR01NS050452 · NINDS · UNIVERSITY OF CENTRAL FLORIDA · PI HICKMAN, JAMES J · 2005 to 2020
$6.4M
Optical microresonator biosensors for high-throughput, real-time analysis of cellR01GM095906 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI VOLLMER, FRANK · 2011 to 2015
$1.8M
High-throughput Electrophysiology for Pathway IdentificationR01EB005459 · NIBIB · UNIVERSITY OF CENTRAL FLORIDA · PI HICKMAN, JAMES J · 2006 to 2008
$1.3M
NIBIB NIH HHS R01 EB005459NIBIB NIH HHS R01EB005459NIGMS NIH HHS 1R01GM095906-01NIGMS NIH HHS R01 GM095906NINDS NIH HHS R01 NS050452NINDS NIH HHS R01NS050452
6 · The paper itself

Abstract

Understanding protein adsorption and resultant conformation changes on modified and unmodified silicon dioxide surfaces is a subject of keen interest in biosensors, microfluidic systems and for medical diagnostics. However, it has been proven difficult to investigate the kinetics of the adsorption process on these surfaces as well as understand the topic of the denaturation of proteins and its effect on enzyme activity. A highly sensitive optical whispering gallery mode (WGM) resonator was used to study a catalytic enzyme's adsorption processes on different silane modified glass substrates (plain glass control, DETA, 13 F, and SiPEG). The WGM sensor was able to obtain high resolution kinetic data of glucose oxidase (GO) adsorption with sensitivity of adsorption better than that possible with SPR. The kinetic data, in combination with a functional assay of the enzyme activity, was used to test hypotheses on adsorption mechanisms. By fitting numerical models to the WGM sensograms for protein adsorption, and by confirming numerical predictions of enzyme activity in a separate assay, we were able to identify mechanisms for GO adsorption on different alkylsilanes and infer information about the adsorption of protein on nanostructured surfaces.

Indexed as

Models, ChemicalAdsorptionBiosensing TechniquesComputer SimulationEnzyme ActivationEquipment DesignEquipment Failure AnalysisGlucose OxidaseMicro-Electrical-Mechanical SystemsModels, MolecularProtein DenaturationSurface Plasmon ResonanceSystems IntegrationGlucose OxidaseBiosensorModelingNanobiotechnologyProtein adsorptionSelf-assembled monolayerSurface modification

Identifiers

PMID25453976
PMCPMC4254915
OpenAlexW2134260527

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.