Evidence map›Paper›PMID 23469929›Full record

ArticleAnalytical chemistry2013

Single nanoparticle detection for multiplexed protein diagnostics with attomolar sensitivity in serum and unprocessed whole blood.

Margo R Monroe, George G Daaboul, Ahmet Tuysuzoglu, Carlos A Lopez, Frédéric F Little, M Selim Unlü

Open access · greenAbstract readEvaluation Study
In one paragraph

Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 81 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Margo R MonroeDepartment of Biomedical Engineering, Boston University, Boston, Massachusetts 02215, United States.
George G Daaboul
Ahmet Tuysuzoglu
Carlos A Lopez
Frédéric F Little
M Selim Unlü
Boston University · US

Funding

Rapid Fluorescence-Based Determination of Antibiotic SusceptibilityU54EB015408 · NIBIB · MASSACHUSETTS GENERAL HOSPITAL · PI PARRISH, JOHN A, SCHACHTER, STEVEN · 2012 to 2022
$49.2M
Boston University Cross-Disciplinary Training in Nanotechnology for CancerR25CA153955 · NCI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI FALLER, DOUGLAS V, GOLDBERG, BENNETT B · 2010 to 2014
$2.1M
Multiplexed, Rapid, Point of Care Device to Quantify Specific IgE to Common AllerR21EB015900 · NIBIB · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI UNLU, M SELIM · 2012 to 2013
$398k
NCI NIH HHS R25 CA153955NIBIB NIH HHS R21 EB015900NIBIB NIH HHS R21EB015900NIBIB NIH HHS U54 EB015408
6 · The paper itself

Abstract

Although biomarkers exist for a range of disease diagnostics, a single low-cost platform exhibiting the required sensitivity, a large dynamic-range and multiplexing capability, and zero sample preparation remains in high demand for a variety of clinical applications. The Interferometric Reflectance Imaging Sensor (IRIS) was utilized to digitally detect and size single gold nanoparticles to identify protein biomarkers in unprocessed serum and blood samples. IRIS is a simple, inexpensive, multiplexed, high-throughput, and label-free optical biosensor that was originally used to quantify biomass captured on a surface with moderate sensitivity. Here we demonstrate detection of β-lactoglobulin, a cow's milk whey protein spiked in serum (>10 orders of magnitude) and whole blood (>5 orders of magnitude), at attomolar sensitivity. The clinical utility of IRIS was demonstrated by detecting allergen-specific IgE from microliters of characterized human serum and unprocessed whole blood samples by using secondary antibodies against human IgE labeled with 40 nm gold nanoparticles. To the best of our knowledge, this level of sensitivity over a large dynamic range has not been previously demonstrated. IRIS offers four main advantages compared to existing technologies: it (i) detects proteins from attomolar to nanomolar concentrations in unprocessed biological samples, (ii) unambiguously discriminates nanoparticles tags on a robust and physically large sensor area, (iii) detects protein targets with conjugated very small nanoparticle tags (~40 nm diameter), which minimally affect assay kinetics compared to conventional microparticle tagging methods, and (iv) utilizes components that make the instrument inexpensive, robust, and portable. These features make IRIS an ideal candidate for clinical and diagnostic applications.

Indexed as

AnimalsBiosensing TechniquesCattleGoldHumansImmunoglobulin EInterferometryLactoglobulinsMilkMilk ProteinsNanoparticlesSensitivity and SpecificityWhey ProteinsGoldImmunoglobulin ELactoglobulinsMilk ProteinsWhey Proteins

Identifiers

PMID23469929
PMCPMC3690328
OpenAlexW2007455368

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.