Evidence map›Paper›PMID 35852494›Full record

ArticleAnalytical chemistry2022

Label-Free Imaging of Single Proteins and Binding Kinetics Using Total Internal Reflection-Based Evanescent Scattering Microscopy.

Pengfei Zhang, Rui Wang, Zijian Wan, Xinyu Zhou, Guangzhong Ma, Jayeeta Kolay, Jiapei Jiang, Shaopeng Wang

Abstract read
In one paragraph

Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

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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

8 authors.

Pengfei ZhangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, Arizona 85287, United States.ORCID 0000-0002-3595-0490
Rui WangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, Arizona 85287, United States.ORCID 0000-0002-9452-9241
Zijian WanBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, Arizona 85287, United States.ORCID 0000-0001-7923-6451
Xinyu ZhouBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, Arizona 85287, United States.ORCID 0000-0003-1399-828X
Guangzhong MaBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, Arizona 85287, United States.ORCID 0000-0002-1197-659X
Jayeeta KolayBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, Arizona 85287, United States.
Jiapei JiangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, Arizona 85287, United States.
Shaopeng WangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, Arizona 85287, United States.ORCID 0000-0002-2680-0503

Funding

Quantitative label-free imaging of membrane protein interaction kinetics on cellsR01GM107165 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI WANG, SHAOPENG · 2014 to 2021
$2.2M
NIGMS NIH HHS R01 GM107165
6 · The paper itself

Abstract

Single-molecule detection can push beyond ensemble averages and reveal the statistical distributions of molecular properties. Measuring the binding kinetics of single proteins also represents one of the critical and challenging tasks in protein analysis. Here, we report total internal reflection-based evanescent scattering microscopy with label-free single-protein detection capability. Total internal reflection is employed to excite the evanescent field to enhance light-analyte interaction and reduce environmental noise. As a result, the system provides wide-field imaging capability and allows excitation and observation using one objective. In addition, this system quantifies protein binding kinetics by simultaneously counting the binding of individual molecules and recording their binding sites with nanometer precision, providing a digital method to measure binding kinetics with high spatiotemporal resolution. This approach does not employ specially designed microspheres or nanomaterials and may pave a way for label-free single-protein analysis in conventional microscopy.

Indexed as

NanostructuresMicroscopy, Fluorescence

Identifiers

PMID35852494
PMCPMC9467297

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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.