Evidence map›Paper›PMID 25058939›Full record

ArticleBiosensors & bioelectronics2015

Overcoming the aggregation problem: a new type of fluorescent ligand for ConA-based glucose sensing.

Brian M Cummins, Mingchien Li, Andrea K Locke, David J S Birch, Gyula Vigh, Gerard L Coté

Abstract read
In one paragraph

Article in Biosensors & bioelectronics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

10 citing papers in PubMed, 18 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 2 institutions in 2 countries.

Brian M CumminsDepartment of Biomedical Engineering, Texas A&M University, College Station, TX 77843, USA; Department of Physics, University of Strathclyde, Glasgow G1 1XQ, UK. Electronic address: bmcummins@ncsu.edu.
Mingchien LiDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Andrea K LockeDepartment of Biomedical Engineering, Texas A&M University, College Station, TX 77843, USA.
David J S BirchDepartment of Physics, University of Strathclyde, Glasgow G1 1XQ, UK.
Gyula VighDepartment of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Gerard L CotéDepartment of Biomedical Engineering, Texas A&M University, College Station, TX 77843, USA.
Texas A&M University · USUniversity of Strathclyde · GB

Funding

A Self-Cleaning Membrane to Extend the Lifetime of an Implanted Glucose BiosensorR01DK095101 · NIDDK · TEXAS ENGINEERING EXPERIMENT STATION · PI GRUNLAN, MELISSA · 2012 to 2016
$1.6M
ROLE(S) OF THE VENTROMEDIAL NUCLEI IN HPA AXIS FUNCTIONF32DK009510 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI CHOI, SUJEAN · 1996 to 1998
–
NIDDK NIH HHS F32 DK009510NIDDK NIH HHS R01DK09510NIDDK NIH HHS R01 DK095101
6 · The paper itself

Abstract

Competitive binding assays based on the lectin Concanavalin A (ConA) have displayed significant potential to serve in continuous glucose monitoring applications. However, to date, this type of fluorescent, affinity-based assay has yet to show the stable, glucose predictive capabilities that are required for such an application. This instability has been associated with the extensive crosslinking between traditionally-used fluorescent ligands (presenting multiple low-affinity moieties) and ConA (presenting multiple binding sites) in free solution. The work herein introduces the design and synthesis of a new type of fluorescent ligand that can avoid this aggregation and allow the assay to be sensitive across the physiologically relevant glucose concentration range. This fluorescent ligand (APTS-MT) presents a single high-affinity trimannose moiety that is recognized by ConA's full binding site and a fluorophore that can effectively track the ligand's equilibrium binding via fluorescent anisotropy. This is confirmed by comparing its measured fluorescent lifetime to experimentally-determined rotational correlation lifetimes of the free and bound populations. Using an assay comprised of 200 nM APTS-MT and 1 µM ConA, the fluorescence anisotropy capably tracks the concentration of monosaccharides that are known to bind to ConA's primary binding site, and the assay displays a MARD of 6.5% across physiologically relevant glucose concentrations. Ultimately, this rationally-designed fluorescent ligand can facilitate the realization of the full potential of ConA-based glucose sensing assays and provide the basis for a new set of competing ligands to be paired with ConA.

Indexed as

Binding, CompetitiveBinding SitesBiosensing TechniquesConcanavalin AFluorescence PolarizationGlucoseLigandsConcanavalin AGlucoseLigandsAffinityBiosensorCompetitive bindingConcanavalin AFluorescence anisotropyGlucose sensing

Identifiers

PMID25058939
PMCPMC5106187
OpenAlexW2042298220

What OpenQuestion holds

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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.