Evidence map›Paper›PMID 26812111›Full record

ArticleInternational journal of biological macromolecules2016

The effect of pH on the glucose response of the glucose-galactose binding protein L255C labeled with Acrylodan.

Mayyada M H El-Sayed, Sheniqua R Brown, KarunaSri Mupparapu, Leah Tolosa

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of biological macromolecules, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
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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

4 authors.

Mayyada M H El-SayedCenter for Advanced Sensor Technology, Department of Chemical and Biochemical Engineering, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, United States. Electronic address: mayyada@aucegypt.edu.
Sheniqua R BrownCenter for Advanced Sensor Technology, Department of Chemical and Biochemical Engineering, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, United States. Electronic address: sbrown12@umbc.edu.
KarunaSri MupparapuCenter for Advanced Sensor Technology, Department of Chemical and Biochemical Engineering, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, United States. Electronic address: karunam@umbc.edu.
Leah TolosaCenter for Advanced Sensor Technology, Department of Chemical and Biochemical Engineering, University of Maryland, Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, United States. Electronic address: leah@umbc.edu.

Funding

Engineered Proteins for Continuous Metabolic MonitoringR01DK072465 · NIDDK · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI TOLOSA, LEAH · 2005 to 2009
$1.3M
Assessing feeding practices, immune activation, and HIV risk in African infantsK08HD069201 · NICHD · SEATTLE CHILDREN'S HOSPITAL · PI JASPAN, HEATHER BERYL · 2011 to 2015
$644k
Noninvasive neonatal glucose monitorR41HD069207 · NICHD · FLUOROMETRIX CORPORATION · PI POTTS, RUSSELL O, TOLOSA, LEAH · 2011 to 2012
$463k
NICHD NIH HHS K08 HD069201NICHD NIH HHS R41HD069201NICHD NIH HHS R41 HD069207NIDDK NIH HHS R01 DK072465NIDDK NIH HHS R01DK072465
6 · The paper itself

Abstract

The glucose-galactose binding protein (GGBP) is used as an optical biosensor in medical and bioprocess applications. This paper investigates the effect of pH on the behavior of GGBP-L255C labeled with Acrylodan for the purpose of finding the optimum conditions for sensing purposes as well as for protein preparation, purification and storage. The Acrylodan-GGBP fluorescence response in absence and presence of glucose was measured under varying buffer and pH conditions. Dissociation constants (Kd) and Gibbs free energies (ΔG) for the protein-glucose binding were calculated. Binding was found to be energetically favored at slightly acidic to neutral conditions, specifically close to the pI of GBP (∼ 5.0). Minimal fluorescence response to glucose was exhibited at pH 3.0 accompanied by a blue shift in the steady state fluorescence spectrum. In contrast, an almost 45% response to glucose was shown at pH 4.5-9.0 with a 13-nm red shift. Frequency domain lifetime measurements and quenching with KI suggest that at highly acidic conditions both the glucose-free and the glucose-bound protein are in a conformation distinct from those observed at higher pH values.

Indexed as

2-NaphthylamineBiosensing TechniquesCalcium-Binding ProteinsGlucoseHydrogen-Ion ConcentrationMonosaccharide Transport ProteinsPeriplasmic Binding Proteins2-NaphthylamineacrylodanCalcium-Binding Proteinsgalactose-binding proteinGlucoseMonosaccharide Transport ProteinsPeriplasmic Binding ProteinsBiosensorDissociation constantFluorescenceGlucose-binding proteinLifetime measurementspH effect

Identifiers

PMID26812111
PMCPMC4809043

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.