Evidence map›Paper›PMID 38558786›Full record

ArticleSensors and actuators. B, Chemical2024

Assessing Aptamer-Analyte Binding Kinetics by Microfluidic Fluorescence Microscopy.

Kechun Wen, Xin Meng, Chengxi Wang, Jingyang Zhao, Samantha Botros, Qiao Lin

Open access · greenAbstract read
In one paragraph

Article in Sensors and actuators. B, Chemical, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 40% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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.

Kechun WenDepartment of Mechanical Engineering, Columbia University, New York, NY, 10027, USA.
Xin MengDepartment of Mechanical Engineering, Columbia University, New York, NY, 10027, USA.
Chengxi WangDepartment of Mechanical Engineering, Columbia University, New York, NY, 10027, USA.
Jingyang ZhaoDepartment of Mechanical Engineering, Columbia University, New York, NY, 10027, USA.
Samantha BotrosDepartment of Mechanical Engineering, Columbia University, New York, NY, 10027, USA.
Qiao LinDepartment of Mechanical Engineering, Columbia University, New York, NY, 10027, USA.
Columbia University · US

Funding

Sample Engineering CoreU19AI067773 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI FORNACE, ALBERT J · 2005 to 2024
$105.4M
Towards rapid measurement of antibiotics in critical care settingR01EB032910 · NIBIB · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CREMERS, SERGE, LIN, QIAO · 2022 to 2025
$2.7M
Analog-based Approaches to Isolation of Aptamers for Challenging TargetsR01GM138843 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI STOJANOVIC, MILAN N · 2020 to 2023
$2.3M
A Practical Approach to Tumor-Specific Aptamers for B-Cell Hematologic MalignanciesR21CA261775 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI LIN, QIAO · 2022 to 2024
$599k
NCI NIH HHS R21 CA261775NIAID NIH HHS U19 AI067773NIBIB NIH HHS R01 EB032910NIGMS NIH HHS R01 GM138843
6 · The paper itself

Abstract

Kinetic measurement plays a crucial role in understanding aptamer binding mechanisms and identifying appropriate aptamers for clinical and research applications. Current techniques, while well established, generally require large sample volumes, bulky and expensive instruments operated by trained personnel, and are hence not readily accessible to resource-limited research laboratories. This paper presents a fluorescence microscopy-based microfluidic assay for measuring aptamer-analyte binding kinetics in a simple and cost-effective manner. Kinetic measurements are achieved by monitoring time-course fluorescence of fluorescently labeled aptamers as they bind to the targets trapped in a microfluidic chip. Fluorescence measurements are performed on a standard fluorescence microscope and are accessible to laboratories with only modest resources. Moreover, microfluidic technology allows efficient and cost-effective immobilization of small amounts of target molecules or live cells as well as flow-based manipulation of aptamers for the measurements. Kinetic measurements of aptamer binding to immunoglobulin E protein and CCRF-CEM cells have yielded results consistent with those obtained from established methods, demonstrating the potential utility of our method for exploring aptamer-target interactions and identifying aptamers that best suit specific given biomedical applications.

Indexed as

aptamerfluorescence microscopykineticsmicrofluidics

Identifiers

PMID38558786
PMCPMC10977918
OpenAlexW4388806344

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.