ArticleACS chemical biology2014
Glucose recognition proteins for glucose sensing at physiological concentrations and temperatures.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- From weak adsorption to selective detection: functionalized interfaces for SERS glucose sensing.RSC advances · 2026Review
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- 3D Printed Hydrogel Microneedle Arrays for Interstitial Fluid Biomarker Extraction and Colorimetric Detection.Polymers · 2023Article
- Microneedle Patches Loaded with Nanovesicles for Glucose Transporter-Mediated Insulin Delivery.ACS nano · 2022Article
- Protein sensors combining both on-and-off model for antibody homogeneous assay.Biosensors & bioelectronics · 2022Article
- Reagentless electrochemical biosensors through incorporation of unnatural amino acids on the protein structure.Biosensors & bioelectronics · 2022Article
- Minimally invasive technique for measuring transdermal glucose with a fluorescent biosensor.Analytical and bioanalytical chemistry · 2018Article
- Bioresponsive Microneedles with a Sheath Structure for HSmall (Weinheim an der Bergstrasse, Germany) · 2018Article
- Article
- Glucose monitoring in living cells with single fluorescent protein-based sensors.RSC advances · 2018Article
- Transcriptional regulatory proteins as biosensing tools.Chemical communications (Cambridge, England) · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Advancements in biotechnology have allowed for the preparation of designer proteins with a wide spectrum of unprecedented chemical and physical properties. A variety of chemical and genetic methods can be employed to tailor the protein's properties, including its stability and various functions. Herein, we demonstrate the production of semisynthetic glucose recognition proteins (GRPs) prepared by truncating galactose/glucose binding protein (GBP) of E. coli and expanding the genetic code via global incorporation of unnatural amino acids into the structure of GBP and its fragments. The unnatural amino acids 5,5,5-trifluoroleucine (FL) and 5-fluorotryptophan (FW) were chosen for incorporation into the proteins. The resulting semisynthetic GRPs exhibit enhanced thermal stability and increased detection range of glucose without compromising its binding ability. These modifications enabled the utilization of the protein for the detection of glucose within physiological concentrations (mM) and temperatures ranging from hypothermia to hyperthermia. This ability to endow proteins such as GBP with improved stability and properties is critical in designing the next generation of tailor-made biosensing proteins for continuous in vivo glucose monitoring.
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Registered trials
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.