Evidence map›Paper›PMID 25793408›Full record

ArticlePloS one2015

The interaction affinity between vascular cell adhesion molecule-1 (VCAM-1) and very late antigen-4 (VLA-4) analyzed by quantitative FRET.

Sandeep Chakraborty, Shih-Yang Hu, Shu-Han Wu, Artashes Karmenyan, Arthur Chiou

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

19 citing papers in PubMed, 22 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

5 authors at 2 institutions in 1 country.

Sandeep ChakrabortyInstitute of Biophotonics, National Yang-Ming University, Taipei, Taiwan, 11221, ROC.
Shih-Yang HuInstitute of Biophotonics, National Yang-Ming University, Taipei, Taiwan, 11221, ROC.
Shu-Han WuInstitute of Biophotonics, National Yang-Ming University, Taipei, Taiwan, 11221, ROC; Research Center for Applied Sciences, Academia Scinica, Taipei, Taiwan, 11529, ROC.
Artashes KarmenyanDepartment of Physics, National Dong Hwa University, Hualien, Taiwan, 97401, ROC; Biophotonics & Molecular Imaging Research Center, National Yang-Ming University, Taipei, Taiwan, 11221, ROC.
Arthur ChiouInstitute of Biophotonics, National Yang-Ming University, Taipei, Taiwan, 11221, ROC; Biophotonics & Molecular Imaging Research Center, National Yang-Ming University, Taipei, Taiwan, 11221, ROC.
National Yang Ming Chiao Tung University · TWNational Dong Hwa University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Very late antigen-4 (VLA-4), a member of integrin superfamily, interacts with its major counter ligand vascular cell adhesion molecule-1 (VCAM-1) and plays an important role in leukocyte adhesion to vascular endothelium and immunological synapse formation. However, irregular expressions of these proteins may also lead to several autoimmune diseases and metastasis cancer. Thus, quantifying the interaction affinity of the VCAM-1/VLA-4 interaction is of fundamental importance in further understanding the nature of this interaction and drug discovery. In this study, we report an 'in solution' steady state organic fluorophore based quantitative fluorescence resonance energy transfer (FRET) assay to quantify this interaction in terms of the dissociation constant (Kd). We have used, in our FRET assay, the Alexa Fluor 488-VLA-4 conjugate as the donor, and Alexa Fluor 546-VCAM-1 as the acceptor. From the FRET signal analysis, Kd of this interaction was determined to be 41.82 ± 2.36 nM. To further confirm our estimation, we have employed surface plasmon resonance (SPR) technique to obtain Kd = 39.60 ± 1.78 nM, which is in good agreement with the result obtained by FRET. This is the first reported work which applies organic fluorophore based 'in solution' simple quantitative FRET assay to obtain the dissociation constant of the VCAM-1/VLA-4 interaction, and is also the first quantification of this interaction. Moreover, the value of Kd can serve as an indicator of abnormal protein-protein interactions; hence, this assay can potentially be further developed into a drug screening platform of VLA-4/VCAM-1 as well as other protein-ligand interactions.

Indexed as

Fluorescence Resonance Energy TransferHumansIntegrin alpha4beta1KineticsProtein BindingSpectrophotometry, UltravioletSurface Plasmon ResonanceVascular Cell Adhesion Molecule-1Integrin alpha4beta1Vascular Cell Adhesion Molecule-1

Identifiers

PMID25793408
PMCPMC4368157
OpenAlexW2004896194

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Registered trials

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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.