Last update 01 Nov 2024

Cholesterol x COX

Last update 01 Nov 2024

Basic Info

Related Targets

CholesterolCOX

Drugs associated with Cholesterol x COX

SC-108

Target

COX x Cholesterol

Mechanism

COX inhibitors [+2]

Active Org.-

Originator Org.

Scotia

Active Indication-

Inactive Indication

Coronary Restenosis [+1]

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with Cholesterol x COX

100 Translational Medicine associated with Cholesterol x COX

0 Patents (Medical) associated with Cholesterol x COX

Literatures (Medical) associated with Cholesterol x COX

01 Nov 2018·TalantaQ2 · CHEMISTRY

A single step electrochemical integration of gold nanoparticles, cholesterol oxidase, cholesterol esterase and mediator with polypyrrole films for fabrication of free and total cholesterol nanobiosensors

Q2 · CHEMISTRY

Article

Author: Rahim, Mohd Zulkhairi Abdul ; Govender-Hondros, Gwen ; Adeloju, Samuel B

The development of free and total cholesterol nanobiosensors based on a single step electrochemical integration of gold nanoparticles (AuNPs), cholesterol oxidase (COx), cholesterol esterase (CE) and a mediator with polypyrrole (PPy) films is described. The incorporation of the various components in the PPy films was confirmed by chronopotentiometry, cyclic voltammetry (CV), scanning electron microscopy, energy dispersive X-ray analysis (SEM-EDX), and Fourier transformed infrared (FTIR) spectroscopy. The free cholesterol, PPy-NO₃^--Fe(CN)₆^4--AuNPs-COx, nanobiosensor achieved a minimum detectable concentration of 5 μM, a linear concentration range of 5-25 μM and a sensitivity of 1.6 µA cm^-2 µM^-1 in 0.05 M phosphate buffer (pH 7.00). For the total cholesterol, PPy-NO₃^--Fe(CN)₆^4--AuNPs-COx-CE, nanobiosensor which also involved the co-incorporation of cholesterol esterase (CE) with the other components, the achieved performances include a minimum detectable total cholesterol concentration of 25 μM, a broader linear concentration range of 25-170 μM and a lower sensitivity of 0.1 µA µM^-1 cm^-2. Owing to its high selectivity, the presence of common interferants did not affect the total cholesterol measurement with the PPy-NO₃^--Fe(CN)₆^4--AuNPs-COx-CE nanobiosensor. Both nanobiosensors were successfully used for direct and indirect determination of total cholesterol in human blood serum samples.

01 Jan 2016·Applied Biochemistry and BiotechnologyQ3 · ENGINEERING & TECHNOLOGY

Purification and Characterization of an Extracellular Cholesterol Oxidase of Bacillus subtilis Isolated from Tiger Excreta

Q3 · ENGINEERING & TECHNOLOGY

Article

Author: Kumari, Lata ; Kanwar, Shamsher S

A mesophilic Bacillus sp. initially isolated from tiger excreta and later identified as a Bacillus subtilis strain was used to produce an extracellular cholesterol oxidase (COX) in cholesterol-enriched broth. This bacterial isolate was studied for the production of COX by manipulation of various physicochemical parameters. The extracellular COX was successfully purified from the cell-free culture broth of B. subtilis by successive salting out with ammonium sulfate, dialysis, and riboflavin-affinity chromatography. The purified COX was characterized for its molecular mass/structure and stability. The enzyme possessed some interesting properties such as high native Mr (105 kDa), multimeric (pentamer of ∼21 kDa protein) nature, organic solvent compatibility, and a half-life of ∼2 h at 37 °C. The bacterial COX exhibited ∼22 % higher activity in potassium phosphate buffer (pH 7.5) in the presence of a nonionic detergent Triton X-100 at 0.05 % (v/v). The K m and V max value of COX of B. subtilis COX were found to be 3.25 mM and 2.17 μmol min ml(-1), respectively. The purified COX showed very little cytotoxicity associated with it.

01 Dec 2001·Biosensors and BioelectronicsQ1 · ENGINEERING & TECHNOLOGY

Cholesterol biosensors prepared by layer-by-layer technique

Q1 · ENGINEERING & TECHNOLOGY

Article

Author: Manoj Ku. Ram ; Claudio Nicolini ; Paolo Bertoncello ; H. Ding ; Sergio Paddeu

The analysis of formation, deposition and characterization of cholesterol oxidase (COX) layer-by-layer films were performed. Initially, a layer of polyanion, poly(styrene sulfonate) (PSS) was adsorbed followed by a layer of polycation, poly(ethylene imine) (PEI) on each solid substrate from aqueous solutions. The alternating layers were formed by consecutive adsorption of polycations (PEI) and negatively charged proteins (COX) and cholesterol esterase (CE). A strong interaction between protein and polyelectrolyte improves the stability of the alternating multilayer; however, it can change a native protein conformation and impair the protein activity. The PSS/PEI/COX, PSS/PEI/COX/PEI/CE, PSS/PEI/COX-CE/PEI etc. layered structures were prepared on the surface of a platinum electrode, ITO coated glass plate, quartz crystal microbalance, quartz plates, mica and silicon substrates. Optical and gravimetric measurements based on an ultraviolet-visible absorption spectroscopy and a quartz crystal microbalance revealed that the enzyme multilayers thus prepared consist of molecular layered of the proteins. The surface morphology of such bilayer films was investigated by using atomic force microscopy. The electrochemical redox processes of the enzyme-layered films deposited either on platinum or ITO coated glass plate were investigated. The response current of cholesterol oxidase electrode with concentration of cholesterol was investigated at length.

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