An Enantioselective Fluorescence Sensor for Glucose Based on a Cyclic Tetrapeptide Containing Two Boronic Acid Binding Sites

2006 ◽  
Vol 2006 (18) ◽  
pp. 4177-4186 ◽  
Author(s):  
Guido Heinrichs ◽  
Marc Schellenträger ◽  
Stefan Kubik
Keyword(s):  
Binding Sites ◽  
Boronic Acid ◽  
Fluorescence Sensor ◽  
Cyclic Tetrapeptide

scholarly journals Ditopic boronic acid and imine-based naphthalimide fluorescence sensor for copper(ii)

2014 ◽  
Vol 50 (80) ◽  
pp. 11806-11809 ◽  
Author(s):  
Meng Li ◽  
Haobo Ge ◽  
Rory L. Arrowsmith ◽  
Vincenzo Mirabello ◽  
Stanley W. Botchway ◽  
...  
Keyword(s):  
Boronic Acid ◽  
Fluorescence Sensor

Luminescent behavior of pyrene-allied calix[4]arene for the highly pH-selective recognition and determination of Zn2+, Hg2+ and I−via the CHEF-PET mechanism: computational experiment and paper-based device

2019 ◽  
Vol 43 (25) ◽  
pp. 9855-9864 ◽  
Author(s):  
Pinkesh G. Sutariya ◽  
Heni Soni ◽  
Sahaj A. Gandhi ◽  
Alok Pandya
Keyword(s):  
Binding Sites ◽  
Computational Experiment ◽  
Fluorescence Sensor ◽  
Selective Recognition ◽  
First Time ◽  
Luminescent Behavior

In this article, for the first time, we have reported a novel CHEF-PET fluorescence sensor L based on calix[4]arene containing four pyrene groups as binding sites, which is highly selective and sensitive towards Zn2+, Hg2+ and I−.

scholarly journals Tetra-porphyrin molecular tweezers: two binding sites linked via a polycyclic scaffold and rotating phenyl diimide core

2016 ◽  
Vol 14 (37) ◽  
pp. 8707-8720 ◽  
Author(s):  
R. B. Murphy ◽  
R. E. Norman ◽  
J. M. White ◽  
M. V. Perkins ◽  
M. R. Johnston
Keyword(s):  
Binding Sites ◽  
Boronic Acid ◽  
Molecular Tweezers

Tetra-porphyrin molecular tweezers linked by rigid polycyclic arms, capable of interannular cooperativity, are synthesised using imide–boronic acid coupling.

A Ditopic Fluorescence Sensor for Saccharides and Mercury Based on a Boronic-Acid Receptor and Desulfurisation Reaction

2011 ◽  
Vol 6 (11) ◽  
pp. 3054-3058 ◽  
Author(s):  
Zhitao Xing ◽  
Hui-Chen Wang ◽  
Yixiang Cheng ◽  
Tony D. James ◽  
Chengjian Zhu
Keyword(s):  
Boronic Acid ◽  
Fluorescence Sensor ◽  
Acid Receptor

scholarly journals 727. Potency of the β-Lactamase Inhibitor QPX7728 Is Minimally Affected by KPC Mutations that Reduce Potency of Ceftazidime–Avibactam

2019 ◽  
Vol 6 (Supplement_2) ◽  
pp. S326-S326 ◽  
Author(s):  
Olga Lomovskaya ◽  
Kirk J Nelson ◽  
Debora Rubio-Aparicio
Keyword(s):  
Binding Sites ◽  
Boronic Acid ◽  
Fold Increase ◽  
The United States ◽  
Microdilution Method ◽  
Carbapenem Resistant ◽  
Broth Microdilution Method ◽  
Lactamase Inhibitor ◽  
Carbapenem Resistant Enterobacteriaceae

Abstract Background In the United States, carbapenem-resistant Enterobacteriaceae (CRE) are mainly represented by KPC-producing strains and ceftazidime–avibactam (C/A) is increasingly used to treat infections caused by KPC-producers. C/A resistant (C/A-R) mutants with mutations in blaKPC can be isolated in vitro and were reported in patients treated with C/A. QPX7728 (QPX) is a new ultra-broad-spectrum β-lactamase inhibitor based on a cyclic boronic acid pharmacophore with a potent activity against serine and metallo-β-lactamases. QPX in combination with meropenem (MER), M/Q, or cefepime (FEP), F/Q, has potent activity against all types of CRE (KPC, MBLs and OXA-48). The objective of these studies was to evaluate the activity of QPX in combination with various antibiotics against KPC-producing strains with C/A-R due to mutations in blaKPC. Methods Ten strains of KPC-producing Klebsiella pneumoniae with C/A MIC varied from 0.5 µg/mL to 8 µg/mL were used in resistance studies using C/A at 2x–8x the MIC (with avibactam [AVI] fixed at 4 µg/mL). Mutations in blaKPC were identified by sequence analysis. Ceftazidime (CAZ), MER and FEP MIC alone and with AVI and QPX (both BLIs at 4 µg/mL) were determined using the reference broth microdilution method. Five C/A-R clinical isolates with mutations in blaKPC were also included in the panel. Results Mutations in blaKPC that result in C/A resistance were selected in all strains. Mutants had 4- to 64-fold (16-fold average) increase in C/A MIC that varied from 16 to 128 μg/mL. In contrast, there was a 2-fold increase for CAZ-QPX MICs (MICs between ≤0.125 to 2 μg/mL. Similarly, there was no more than 2-fold increase in MER/QPX and FEP/QPX MICs, and the majority of mutants did not have an increase in MER/QPX or FEP/QPX MICs (MICs varied from ≤0.125 to 1 µg/mL). For five clinical C/A-R isolates, C/A, M/Q and F/Q MIC varied from 16 to ≥128 μg/mL, ≤0.125 to 4 μg/mL, and ≤0.125 to 2 μg/mL, respectively. Conclusion These data indicate that KPC mutations that affect the potency of C/A have minimal effect on the potency of QPX7728 combinations with either CAZ, MER or FEP indicating the potential differences in binding sites for these inhibitors in KPC. Further studies of QPX combinations are in progress. Disclosures All authors: No reported disclosures.

A Glucose-Selective Fluorescence Sensor Based on Boronic Acid-Diol Recognition.

ChemInform ◽  
2003 ◽  
Vol 34 (11) ◽  
Author(s):  
Vishnu Vardhan Karnati ◽  
Xingming Gao ◽  
Shouhai Gao ◽  
Wenqian Yang ◽  
Weijuan Ni ◽  
...  
Keyword(s):  
Boronic Acid ◽  
Fluorescence Sensor

Conformation of Ribosomes from Escherichia Coli

1974 ◽  
Vol 32 ◽  
pp. 210-211
Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Binding Sites ◽  
Ribosomal Proteins ◽  
Fluorescent Dyes ◽  
Protein Biosynthesis ◽  
Three Dimensional ◽  
Spatial Arrangement ◽  
Dimensional Structure ◽  
Complete Understanding ◽  
And Function

The present knowledge of the three-dimensional structure of ribosomes is far too limited to enable a complete understanding of the various roles which ribosomes play in protein biosynthesis. The spatial arrangement of proteins and ribonuclec acids in ribosomes can be analysed in many ways. Determination of binding sites for individual proteins on ribonuclec acid and locations of the mutual positions of proteins on the ribosome using labeling with fluorescent dyes, cross-linking reagents, neutron-diffraction or antibodies against ribosomal proteins seem to be most successful approaches. Structure and function of ribosomes can be correlated be depleting the complete ribosomes of some proteins to the functionally inactive core and by subsequent partial reconstitution in order to regain active ribosomal particles.

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