Evidence map›Paper›PMID 21750834›Full record

ArticleNanoscale2011

Characterization of protein immobilization on nanoporous gold using atomic force microscopy and scanning electron microscopy.

Yih Horng Tan, John R Schallom, N Vijaya Ganesh, Kohki Fujikawa, Alexei V Demchenko, Keith J Stine

Abstract read
In one paragraph

Article in Nanoscale, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.6field-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

10 citing papers in PubMed, 43 citations in OpenAlex.

  1. Nanoporous Gold for Enzyme Immobilization.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Facile fabrication of hierarchically nanostructured gold electrode for bio-electrochemical applications.Journal of electroanalytical chemistry (Lausanne, Switzerland) · 2022
    Article
  3. Review
  4. Article
  5. Porous Gold: A New Frontier for Enzyme-Based Electrodes.Nanomaterials (Basel, Switzerland) · 2020
    Review
  6. Article
  7. Lectin-carbohydrate interactions on nanoporous gold monoliths.New journal of chemistry = Nouveau journal de chimie · 2013
    Article
  8. Article
  9. Article
  10. Article
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

6 authors at 1 institution in 1 country.

Yih Horng TanDepartment of Chemistry and Biochemistry, University of Missouri-Saint Louis, Saint Louis, MO 63121, USA.
John R Schallom
N Vijaya Ganesh
Kohki Fujikawa
Alexei V Demchenko
Keith J Stine
University of Missouri–St. Louis · US

Funding

Development and Application of Surface-Tethered Iterative Carbohydrate SynthesisR01GM090254 · NIGMS · UNIVERSITY OF MISSOURI-ST. LOUIS · PI STINE, KEITH J. · 2009 to 2012
$1.1M
NIGMS NIH HHS R01 GM090254NIGMS NIH HHS R01-GM090254
6 · The paper itself

Abstract

Nanoporous gold (NPG), made by dealloying low carat gold alloys, is a relatively new nanomaterial finding application in catalysis, sensing, and as a support for biomolecules. NPG has attracted considerable interest due to its open bicontinuous structure, high surface-to-volume ratio, tunable porosity, chemical stability and biocompatibility. NPG also has the attractive feature of being able to be modified by self-assembled monolayers. Here we use scanning electron microscopy (SEM) and atomic force microscopy (AFM) to characterize a highly efficient approach for protein immobilization on NPG using N-hydroxysuccinimide (NHS) ester functionalized self-assembled monolayers on NPG with pore sizes in the range of tens of nanometres. Comparison of coupling under static versus flow conditions suggests that BSA (Bovine Serum Albumin) and IgG (Immunoglobulin G) can only be immobilized onto the interior surfaces of free standing NPG monoliths with good coverage under flow conditions. AFM is used to examine protein coverage on both the exterior and interior of protein modified NPG. Access to the interior surface of NPG for AFM imaging is achieved using a special procedure for cleaving NPG. AFM is also used to examine BSA immobilized on rough gold surfaces as a comparative study. In principle, the general approach described should be applicable to many enzymes, proteins and protein complexes since both pore sizes and functional groups present on the NPG surfaces are controllable.

Indexed as

AnimalsCattleGoldImmobilized ProteinsImmunoglobulin GMicroscopy, Atomic ForceMicroscopy, Electron, ScanningModels, MolecularNanostructuresNanotechnologyParticle SizePorosityRabbitsSerum Albumin, BovineSuccinimidesSurface PropertiesGoldImmobilized ProteinsImmunoglobulin GN-hydroxysuccinimideSerum Albumin, BovineSuccinimides

Identifiers

PMID21750834
PMCPMC3168530
OpenAlexW2010750750

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.