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1.
J Diabetes Sci Technol ; 9(4): 751-61, 2015 Jul.
Article in English | MEDLINE | ID: mdl-26033921

ABSTRACT

BACKGROUND: Glycemic control in hospital intensive care units (ICU) has been the subject of numerous research publications and debate over the past 2 decades. There have been multiple studies showing the benefit of ICU glucose control in reducing both morbidity and mortality. GlySure Ltd has developed a glucose monitor based on a diboronic acid receptor that can continuously measure plasma glucose concentrations directly in a patient's vascular system. The goal of this study was to validate the performance of the GlySure CIGM system in different patient populations. METHODS: The GlySure Continuous Intravascular Glucose Monitoring (CIGM) System was evaluated in both the Cardiac ICU (33 patients) and MICU setting (14 patients). The sensor was placed through a custom CVC and measured the patients' blood glucose concentration every 15 seconds. Comparison blood samples were taken at 2 hourly then 4 hourly intervals and measured on a YSI 2300 STAT Plus or an i-STAT. RESULTS: Consensus error grid analysis of the data shows that the majority of the data (88.2% Cardiac, and 95.0% MICU) fell within zone A, which is considered to be clinically accurate and all data points fell within zones A and B. The MARD of the Cardiac trial was 9.90% and the MICU trial had a MARD of 7.95%. Data analysis showed no significant differences between data generated from Cardiac and MICU patients or by time or glucose concentration. CONCLUSIONS: The GlySure CIGM System has met the design challenges of measuring intravascular glucose concentrations in critically ill patients with acceptable safety and performance criteria and without disrupting current clinical practice. The accuracy of the data is not affected by the patients' condition.


Subject(s)
Blood Glucose/analysis , Monitoring, Physiologic/instrumentation , Monitoring, Physiologic/methods , Adult , Aged , Aged, 80 and over , Area Under Curve , Catheterization , Critical Care , Diabetes Mellitus/blood , Diabetes Mellitus/diagnosis , Equipment Design , Female , Hospitalization , Humans , Infusions, Intravenous , Intensive Care Units , Male , Middle Aged , Patient Safety , Reference Standards , Reproducibility of Results , Risk , Young Adult
2.
J Org Chem ; 76(16): 6548-57, 2011 Aug 19.
Article in English | MEDLINE | ID: mdl-21732662

ABSTRACT

Contacts between aromatic surfaces and saccharide CH groups are common motifs in natural carbohydrate recognition. These CH-π interactions are modeled in "synthetic lectins" which employ oligophenyl units as apolar surfaces. Here we report the synthesis and study of new synthetic lectins with fluoro- and hydroxy-substituted biphenyl units, designed to explore the role of π-electron density in carbohydrate CH-π interactions. We find evidence that recognition can be moderated through electronic effects but that other factors such as cavity hydration are also important and sometimes predominant in determining binding strengths.


Subject(s)
Biphenyl Compounds/chemistry , Carbohydrates/chemistry , Carbohydrates/chemical synthesis , Lectins/chemistry , Lectins/chemical synthesis , Binding Sites , Crystallography, X-Ray , Electrons , Hydrogen Bonding , Magnetic Resonance Spectroscopy , Models, Molecular
3.
Chem Commun (Camb) ; (43): 6557-9, 2009 Nov 21.
Article in English | MEDLINE | ID: mdl-19865648

ABSTRACT

A fluorescent molecular tweezer for carbohydrates has been prepared which utilises two boronic acid receptor groups.


Subject(s)
Carbohydrates/analysis , Fluorescence
5.
Angew Chem Int Ed Engl ; 48(10): 1775-9, 2009.
Article in English | MEDLINE | ID: mdl-19072969

ABSTRACT

Changing employment: Receptor 1 binds beta-N-acetylglucosaminyl (beta-GlcNAc) up to 100 times more strongly than it does glucose. This synthetic lectin shows affinities similar to wheat germ agglutinin (WGA), a natural lectin used to bind GlcNAc. Remarkably, 1 is more selective than WGA. It favors especially the glycoside unit in glycopeptide 2, a model of the serine-O-GlcNAc posttranslational protein modification.


Subject(s)
Acetylglucosamine/chemistry , Lectins/chemistry , Acetylglucosamine/analogs & derivatives , Acetylglucosamine/metabolism , Amino Acid Sequence , Carbohydrates/chemistry , Kinetics , Lectins/chemical synthesis , Lectins/metabolism , Magnetic Resonance Spectroscopy , Molecular Conformation , Protein Processing, Post-Translational , Wheat Germ Agglutinins/metabolism
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