Evidence map›Paper›PMID 19594133›Full record

ArticleAnalytical chemistry2009

Enhanced fluorescence of proteins and label-free bioassays using aluminum nanostructures.

Krishanu Ray, Henryk Szmacinski, Joseph R Lakowicz

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
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  9. Article
  10. Metal-Enhanced Fluorescence Lifetime Imaging and Spectroscopy on a Modified SERS Substrate.The journal of physical chemistry. C, Nanomaterials and interfaces · 2013
    Article
  11. Article
  12. Article
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  14. Feasibility of Using Bimetallic Plasmonic Nanostructures to Enhance the Intrinsic Emission of Biomolecules.The journal of physical chemistry. C, Nanomaterials and interfaces · 2011
    Article
  15. On the Feasibility of Using the Intrinsic Fluorescence of Nucleotides for DNA Sequencing.The journal of physical chemistry. C, Nanomaterials and interfaces · 2010
    Article
  16. Article
  17. 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

3 authors at 1 institution in 1 country.

Krishanu RayCenter for Fluorescence Spectroscopy, Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 725 West Lombard St, Baltimore, Maryland 21201, USA.
Henryk Szmacinski
Joseph R Lakowicz
University of Maryland, Baltimore · US

Funding

Metallic Surfaces and Particles in DNA AnalysisR01HG002655 · NHGRI · UNIVERSITY OF MARYLAND BALTIMORE · PI LAKOWICZ, JOSEPH R. · 2003 to 2012
$2.8M
Plasmon-Controlled Fluorescence and Cardiac MarkersR01EB006521 · NIBIB · UNIVERSITY OF MARYLAND BALTIMORE · PI LAKOWICZ, JOSEPH R. · 2007 to 2015
$2.7M
Time-resolved fluorometric method for assay of multiple biomarkersR21CA134386 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI SZMACINSKI, HENRYK · 2008 to 2009
$270k
NCI NIH HHS R21 CA134386NCI NIH HHS R21CA134386NHGRI NIH HHS HG002655NHGRI NIH HHS R01 HG002655NIBIB NIH HHS EB006521NIBIB NIH HHS R01 EB006521
6 · The paper itself

Abstract

We report the enhanced intrinsic fluorescence from several proteins in proximity to aluminum nanostructured surfaces. Intrinsic fluorescence in proteins is dominated by the tryptophan residues. Intensities and lifetimes of several proteins with different numbers of tryptophan residues assembled on the surfaces of quartz or aluminum nanostructured films were measured. Immobilized protein molecules on the surface of an aluminum nanostructured film resulted in a significant fluorescence intensity enhancement (up to 14-fold) and lifetime decrease (up to 6-fold) compared to the quartz substrates. These large spectroscopic changes allow design of label-free bioassays where detection of binding interactions between proteins can be observed in the presence of a bulk sample solution. Binding of streptavidin to the biotinylated aluminum surface was demonstrated in the presence of 100 microg/mL bovine serum albumin in the sample solution by measurements of tryptophan intensity and lifetime changes.

Indexed as

Biological AssayFluorescenceNanostructuresAluminumAnimalsBiotinylationCattleMetal NanoparticlesProteinsSerum Albumin, BovineTryptophanAluminumProteinsSerum Albumin, BovineTryptophan

Identifiers

PMID19594133
PMCPMC2846181
OpenAlexW1993482175

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.