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Aminopyridines

Aminopyridines are a class of organic compounds containing a pyridine ring with one or more amino substituents.
These compounds have diverse applications in medicinal chemistry, neuroscience, and materials science.
Aminopyridines exhibit a range of biological activities, including ion channel modulation, neuroprotection, and anti-inflammatory effects.
Researchers studying Aminopyridines can leverage PubCompare.ai's AI-powered platform to easily locate optimized protocols from literature, pre-prjnts, and patents, and leverage AI-driven comparisons to enhance reproducibility and identify the best products for their research needs.
PubCompare.ai's cutting-edge tools can help take your Aminopyridines research to the next level.

Most cited protocols related to «Aminopyridines»

Cortical rat neurons were cultured as described 18 (link) from E21 rats or E17 mouse pups in Neurobasal-A medium and B27 (Invitrogen). Stimulations and transfections (Lipofectamine 2000, Invitrogen) were done at DIV8-10 after transferring neurons into trophically-deprived medium 18 (link). Action potential bursting was induced by treatment with 50 μM bicuculline, plus 250 μM 4-aminopyridine (Sigma) to enhance burst frequency. Stimulations were initiated 12 h prior to the application of an oxidative insult. Neurons were fixed after a further 24 h and subjected to DAPI staining and cell death quantified by counting (blind) the number of apoptotic nuclei as a percentage of the total. For details of analysis of peroxide-induced ROS accumulation and caspase activity, see supplemental methods.
Publication 2008
Action Potentials Aminopyridines Apoptosis Bicuculline Caspase Cell Death Cell Nucleus Cortex, Cerebral DAPI lipofectamine 2000 Mus Neurons Peroxides Rattus norvegicus Transfection Visually Impaired Persons
Reactions were performed with 1 nmol glycopeptide, 2 µL McIlvaine buffer, 0.3 µL enzyme and water added to a final volume of 3.5 µL. Enzymatic reactions for DmFDL were performed at pH 5.5 and 30°C, for AmFDL at pH 5.0 and 37°C. For CeHEX-2, 3 and 4 reactions were performed at pH 6.0 and 37°C. Dabsylated-βGNβGN (glycopeptide carrying two terminal β-linked GalNAc residues) reactions were carried out with excess enzyme (∼2.5 µUnits) for 16 h. In the case of DmFDL and AmFDL, the reactions were performed for a total of 3 days with the addition of excess enzyme every 24 h. Subsequently, 0.5 µL of a dabsylated-βGNβGN glycopeptide reaction mixtures were incubated with 0.25 µL α1,2/3 mannosidase (NEB) and 2 µL McIlvaine buffer pH 5.5 in a total volume of 2.5 µL at room temperature over night. Reactions with dabsylated-GnGn (±core modifications) glycopeptide were performed with enzyme dilutions in order to achieve ∼50% substrate conversion within 2 h. Reactions with 2-aminopyridine labeled glycans (PA-glycans) from C. elegans (prepared as described previously using PNGase A (Paschinger et al. 2012 (link)); for wild type, mixed stages were used, whereas, for the mutant, the predominantly L4 stage was performed by combining 1 µL PA-glycans, 0.5 µL 100 mM ammonium acetate buffer pH 5.0 and 0.5 µL DmFDL enzyme. The reactions were incubated at 30°C for 2 h. All enzymatic reactions were analyzed by an Autoflex Speed MALDI-TOF/TOF MS in positive ion mode using either 1% α-cyano-4-hydroxycinnamic acid (glycopeptides) or 0.3% 6-aza-2-thiothymine (PA-labeled glycans) supplemented with 60 mM NaCl as a matrix.
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Publication 2014
Aminopyridines ammonium acetate Buffers Caenorhabditis elegans Coumaric Acids Enzymes Glycopeptides Mannosidase Polysaccharides Sodium Chloride Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Technique, Dilution

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Publication 2016
Aminopyridines Biological Assay Differential Diagnosis Disaccharides Fluorescence High-Performance Liquid Chromatographies Hyaluronidase Mass Spectrometry Polysaccharides
Cortical mouse neurons were cultured as described (Papadia et al., 2008 (link)) at a density of between 9-13 × 104 neurons per cm2 from E17.5 mice with Neurobasal growth medium supplemented with B27 (Invitrogen). p53-null founder mice were obtained from Dr. Alan Clarke (University of Cardiff, Cardiff, UK) and were extensively crossed into the CD1 background. Puma-null founder mice were obtained from Dr. Andreas Strasser (Villunger et al., 2003 (link)). Stimulations of cultured neurons were done in all cases after a culturing period of 8-10 days during which cortical neurons develop a network of processes, express functional NMDA-type and AMPA/kainate-type glutamate receptors, and form synaptic contacts. Our cultured neurons are 10-15% GABAergic (assessed by immunofluorescence). Bursts of action potential firing were induced by treatment of neurons with 50 μM bicuculline, and burst frequency was enhanced by addition of 250 μM 4-aminopyridine (Hardingham et al., 2001 (link)). MK-801 (used at 10 μM) was from Tocris, TTX (at 2 μM) and 4-aminopyridine from Calbiochem. Neurons were subjected to trophic deprivation by transferring them from growth medium to a medium containing 10% MEM (Invitrogen), 90% Salt-Glucose-Glycine (SGG) medium ((Bading et al., 1993 (link)); SGG: 114 mM NaCl, 0.219 % NaHCO3, 5.292 mM KCl, 1 mM MgCl2, 2 mM CaCl2, 10 mM HEPES, 1 mM Glycine, 30 mM Glucose, 0.5 mM sodium pyruvate, 0.1 % Phenol Red; osmolarity 325 mosm/l,(Papadia et al., 2005 (link))). For this model, apoptosis was analysed after 72 h. Neurons were fixed and subjected to DAPI staining and cell death quantified by counting (blind) the number of apoptotic nuclei as a percentage of the total. Approximately 1500 cells were counted per treatment, across 4 independent experiments (i.e. performed on separate cultures). Morphologically, neurons subjected to trophic deprivation show typical signs of apoptotic-like cell death (shrunken cell body and large round chromatin clumps). Furthermore, death was blocked by the pan-caspase inhibitor Q-VD-Oph (50 μM, Fig. 1a). Chemical inducers of apoptosis were used as follows: staurosporine (Calbiochem, 100 nM), 9-cis retinoic acid (Sigma, 5 μM), okadaic acid (Calbiochem, 2 nM), hydrogen peroxide (Sigma, 100 μM). Cell death in all cases was blocked by pre-treatment with Q-VD-Oph (50 μM, Fig. 1a and (Papadia et al., 2008 (link))). These inducers were applied to neurons for 24 h after which the percentage of apoptotic neurons was analysed as described above.
Publication 2010
Action Potentials Alitretinoin alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid Aminopyridines AMPA Receptors Apoptosis Bicarbonate, Sodium Bicuculline Blindness Caspase Inhibitors Cell Body Cell Death Cell Nucleus Cells Chromatin Cortex, Cerebral Dalfampridine DAPI Glucose Glutamate Glutamate Receptor Glycine HEPES Immunofluorescence Kainate Magnesium Chloride Mice, Knockout MK-801 Mus N-Methylaspartate Neurons Okadaic Acid Osmolarity Peroxide, Hydrogen Puma Pyruvate quinoline-val-asp(OMe)-CH2-OPH Receptors, Kainic Acid Sodium Sodium Chloride Staurosporine
Ictal discharges were induced by injecting 4-aminopyridine (4-AP, Sigma, St. Louis, MO, 15 mM, 0.5 μl) through a single-barreled glass microelectrode using a Nanoject II injector (Drummond Scientific, Broomall, PA). A second single-barreled glass microelectrode (impedance, 2-4 MΩ) filled with 0.9% saline was positioned < 1 mm from the 4-AP electrode and lowered to a depth of 300∼500 μm into the neocortex. Extracellular local field potential (LFP) was amplified and filtered between 0.1 and 500 Hz using a DAB-S system (World Precision Instruments, Sarasota, FL), and digitized at 1000 Hz by a CED Power 1401 (Cambridge Electronic Design, Cambridge, UK). Data was recorded by a PC running the Spike2 software (Cambridge Electronic Design, Cambridge, UK).
Publication 2009
Aminopyridines Cerebrovascular Accident Microelectrodes Neocortex Normal Saline

Most recents protocols related to «Aminopyridines»

Not available on PMC !

Example 185

[Figure (not displayed)]

8-(1-Bromoethyl)-2-(1H-indol-2-yl)-6-(trifluoromethyl)chromen-4-one (0.28 g, 0.64 mmol) and tert-butyl 3-aminopyridine-2-carboxylate (0.19 g, 0.95 mmol) were dissolved in DMF (5 mL) and stirred at 80° C. overnight. The reaction was concentrated and the residue purified by preparative HPLC eluted with 10% to 70% AcCN (0.1% TFA) in water (0.1% TFA) giving the product (6.8 mg, 2.2%). MS ES+ m/z 494 [M+H]+.

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Patent 2024
Aminopyridines High-Performance Liquid Chromatographies picolinic acid TERT protein, human Trifluoroacetic Acid
Not available on PMC !

Example 1

Materials:

Cellulose filter paper (Whatman brand), was used as a cellulose substrate and was dried in a vacuum oven at 65° C. for 14 hours prior to use. 2,2-Bis(hydroxymethyl)propionic acid (Bis-MPA), allyl bromide, thionyl chloride (SOCl2), N,N′-dicyclohexylcarbodiimide (DCC), pyridine, 4-dimethyl(aminopyridine) (DMAP) 1H,1H,2H,2H-perfluorodecanethiol, 1-decanethiol, 2-mercaptoethanol, 2,2-dimethoxy-2-phenyl-acetophenone (DMPA) were purchased from Sigma-Aldrich. Trimethylamine (Et3N), toluene, dichloromethane (DCM), dry DCM and ethyl alcohol were purchased from Bio-lab ltd. Concentrated hydrochloric acid (HCl) and sodium hydroxide (NaOH) pellets were purchased from Merck. All the materials were used as received.

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Patent 2024
2-Mercaptoethanol acetophenone allyl bromide Aminopyridines Anhydrides Cellulose Chlorides Dicyclohexylcarbodiimide Ethanol Hydrochloric acid Methylene Chloride Pellets, Drug propionic acid pyridine Sodium Hydroxide Strains thionyl chloride Toluene trimethylamine Vacuum
Tyrode solution contained (in mM) 140 NaCl, 5 KCl, 2.5 CaCl2, 2 MgCl2, and 10 HEPES. The standard extracellular solution for voltage-clamp experiments contained (in mM) 140 TEA-methane-sulfonate, 2.5 CaCl2, 2 MgCl2, 1 4-aminopyridine, 10 HEPES, and 0.002 tetrodotoxin. For the experiments described in Figs. 1 and 2, the extracellular solution also contained 0.33% DMSO. The standard pipette solution contained (in mM) 120 K-glutamate, 5 Na2-ATP, 5 Na2-phosphocreatine, 5.5 MgCl2, 5 glucose, and 5 HEPES. For measurements of rhod-2 Ca2+ transients, it also contained 15 EGTA, 6 CaCl2, and 0.1 rhod-2. For measurements with fluo-4, isolated muscle fibers were incubated for 30 min in the presence of Tyrode solution containing 10 μM fluo-4 AM. All solutions were adjusted to pH 7.20. The Ringer solution used for muscle force measurements contained (in mM) 140 NaCl, 6 KCl, 3 CaCl2, 2 MgCl2, and 10 HEPES, adjusted to pH 7.40.
Probenecid was prepared as a 0.3 M aliquoted stock solution in DMSO and used in the extracellular solution at 0.5, 1, or 2 mM. Carbenoxolone was prepared as a 10 mM stock solution in the extracellular solution and used at 0.1 mM. These concentrations were chosen on the basis of their effectiveness and wide use to block Panx1 channels throughout the literature (e.g., Dahl et al., 2013 (link)). When testing the effect of either probenecid or carbenoxolone using the preincubation protocol (Figs. 1 and 2), fibers were bathed in the drug-containing extracellular solution from the beginning of the intracellular dialysis with the rhod-2-containing solution (i.e., 30 min before taking measurements). The 10panx1 peptide and the scrambled control peptide (10panx1SCr) were tested under the same conditions at 200 µM while the P2Y2 antagonist AR-C 118925XX was tested at 10 µM. All chemicals and drugs were purchased from Sigma-Aldrich, except for tetrodotoxin (Alomone Labs), rhod-2 and fluo-4 (Thermo Fisher Scientific), and AR-C 118925XX (TOCRIS—Bio-Techne).
In vitro fluorescence measurements using droplets of a solution containing (in mM) 120 K-glutamate, 10 HEPES, 15 EGTA, 6 CaCl2, and 0.1 rhod-2, with or without probenecid, showed that fluorescence intensity in the presence of 1 mM probenecid corresponded to 1.09 ± 0.12% (n = 6) the intensity in the absence of probenecid, excluding an interaction of the drug with the dye to explain the effect on resting fluorescence in muscle fibers.
Publication 2023
Aminopyridines Carbenoxolone Cardiac Arrest Dialysis Solutions Drug Interactions Egtazic Acid Figs Fluo 4 Fluorescence Glucose Glutamate HEPES Magnesium Chloride methanesulfonate Muscle Tissue P2RY2 protein, human Peptides Pharmaceutical Preparations Phosphocreatine Probenecid Protoplasm rhod-2 Ringer's Solution Sodium Chloride Sulfoxide, Dimethyl Tetrodotoxin Transients Tyrode's solution
The ex vivo CAPs were recorded using two glass suction electrodes placed at each end of the dorsal root, one for electrical stimulation and the other for recording. The three main components of the CAP were distinguished based on their activation threshold and conduction velocity as fast (Aαβ), medium (Aδ), and slow (C) conducting components, each displaying a characteristic triphasic (positive–negative–positive) response. To characterize the Aαβ component, dorsal roots were stimulated three times at 0.2 Hz with an ISO-flex stimulus isolator at 0.5–5 μA (in steps of 0.5 μA), 6–14 μA (in steps of 1 μA), and at 15–25 μA (in steps of 5 μA) with a 0.1-ms pulse width.
To measure the Aαβ refractory period (RP), a paired-pulse (0.1-ms wide) stimulation at 25 μA was delivered to the dorsal root with a gradually shortened inter-pulse interval from 20 to 2 ms (in steps of 2 ms). The Aαβ RP is represented as the ratio of the 2nd Aαβ CAP on the 1st Aαβ CAP amplitude (2nd CAP/1st CAP) as a function of the inter-pulse interval. To assess the contribution of Kv1 channels to the RP, following baseline recordings in both WT and KO mice, 500 μM of the Kv1 channel blocker 4-aminopyridine (4-AP) was bath-applied 10 min prior to, and during, a repeated set of RP recordings.
Data were acquired and recorded using an ER-1 differential amplifier and pClamp 10 software. Data were filtered at 10 kHz and sampled at 50 kHz.
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Publication 2023
Aminopyridines Bath Electric Conductivity Mus Pulse Rate Root, Dorsal Stimulations, Electric Suction Drainage Tandem Mass Spectrometry
The biodegradable polymer matrices used in this study were PHB biosynthesized from fructose by Cupriavidus necator strain A-04 according to a previous report [13 (link), 23 (link)]. Batch cultivation was performed in a 10-L bioreactor (MDL-10L, B.E. Marubishi Co., Ltd., Tokyo, Japan). Culture samples were periodically harvested for analysis of the dry cell weight (DCW), PHB, carbon and nitrogen concentrations. The harvested cells were dried, placed in filter paper (Whatman 1002–042, Sigma–Aldrich Corp., St. Louis, MO, USA) and then refluxed in hot chloroform in a Soxhlet apparatus to extract PHBA-04 from the dried cells. The PHBA-04 was precipitated from a chloroform solution using three volumes of n-hexane. The precipitation step was repeated three times [24 , 25 (link)].
As a binder and filler, the agro-industrial residue used in this study was pineapple leaves (Ananas comosus L. Merr.) obtained from Siam Food Products Public Company Limited (Rai Nong Takhian at Tambol Khlong Kaeo, Amphoe Banbung, Chonburi, Thailand). The pineapple leaves were washed repeatedly with distilled water to remove all the dirt, immersed in 5% sodium hypochlorite solution for 1 h, cut into approximately 2 cm × 2 cm pieces, dried in a hot-air oven (UN55, Memmert Co., Ltd., Schwabach, Germany) at 65°C for 24 h, milled using a laboratory blender (45,000 rpm, 1800-W, Healthy mix GP 3.5, Taiwan) and then sieved to fractionate the particle sizes between 0.420 and 0.250 mm (− 40/+ 60 mesh). The chemical composition of the dried pineapple leaves was determined according to the Technical Association of Pulp and Paper Industry (TAPPI) standard methods for the following parameters: benzene extractives (TAPPI T204 cm-07); α-cellulose, β-cellulose, and γ-cellulose (TAPPI T203 om-09); holocellulose (TAPPI T9 m-54; lignin (TAPPI T222 om-15); and ash (TAPPI T-211). Dried pineapple leaves with a particle size of approximately 2 cm × 2 cm were used to extract PALF-MCC.
N,N-Dimethylacetamide (DMAc, RCI Labscan Ltd., Thailand) and anhydrous lithium chloride (LiCl, ≥ 98%, Elago Enterprises Pty Ltd., N.S.W., Australia) were used as solvents, while N,N-dimethyl 1-4-aminopyridine (DMAP, 98%, Fluka) was applied as the catalyst. The esterifying agent was lauroyl chloride (TCI Co., Ltd., Tokyo, Japan). Hydrochloric acid (Merck KGaA, Darmstadt, Germany) was used for hydrolysis, and ethanol (Merck KGaA, Darmstadt, Germany) was used as the precipitating agent.
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Publication 2023
Aminopyridines Ananas Benzene Bioreactors Carbon Cells Cellulose chemical composition Chloride, Lithium Chlorides Chloroform Cupriavidus necator Dental Pulp dimethylacetamide Ethanol Food Fructose Hexanes Hydrochloric acid Hydrolysis Lignin Nitrogen Pineapple Polymers Sodium Hypochlorite Solvents

Top products related to «Aminopyridines»

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4-aminopyridine is a chemical compound used as a laboratory reagent. It is a colorless crystalline solid that is soluble in water and organic solvents. The primary function of 4-aminopyridine is as a research tool for studying ion channels and neurological processes in biological systems.
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4-aminopyridine (4-AP) is a chemical compound used in research and laboratory settings. It serves as a potassium channel blocker, a function that is utilized in various scientific applications. The core purpose of 4-AP is to provide a tool for researchers to investigate and study physiological and biochemical processes.
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4-aminopyridine (4-AP) is a chemical compound used in various research and laboratory applications. It functions as a potassium channel blocker, which can be used to study the role of potassium channels in biological processes.
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The XBridge C18 is a high-performance liquid chromatography (HPLC) column designed for reversed-phase separation of a wide range of analytes. It features a silica-based stationary phase with a C18 alkyl bonding for effective retention and separation of both polar and non-polar compounds.
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BlotGlyco is a lab equipment product developed by Sumitomo Bakelite. It is designed for the analysis and detection of glycoproteins. The core function of BlotGlyco is to facilitate the separation and visualization of glycosylated proteins using electrophoretic techniques.
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Tetrodotoxin (TTX) is a potent neurotoxin that acts as a sodium channel blocker. It is isolated from various marine organisms, including pufferfish. TTX is commonly used in research laboratories for the study of voltage-gated sodium channels and their role in neurophysiology.
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Bicuculline is a laboratory reagent used as a GABA(A) receptor antagonist. It is commonly employed in neuroscience research to study the role of GABA-mediated inhibition in neural circuits and behavior.
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4-Aminopyridine is a chemical compound used as a laboratory reagent. It has the molecular formula C₅H₆N₂. The compound is a crystalline solid at room temperature with a melting point of 156-158°C.
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The Axopatch 200B is a high-performance patch-clamp amplifier designed for electrophysiology research. It is capable of amplifying and filtering electrical signals from single-cell preparations, providing researchers with a tool to study ion channel and membrane properties.
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More about "Aminopyridines"

Aminopyridines are a class of organic compounds containing a pyridine ring with one or more amino substituents, also known as 4-aminopyridine (4-AP) or 4-AP.
These versatile molecules have diverse applications in medicinal chemistry, neuroscience, and materials science, exhibiting a range of biological activities such as ion channel modulation, neuroprotection, and anti-inflammatory effects.
Researchers studying Aminopyridines can leverage PubCompare.ai's AI-powered platform to easily locate optimized protocols from literature, preprints, and patents, and leverage AI-driven comparisons to enhance reproducibility and identify the best products for their research needs.
This includes leveraging related compounds like XBridge C18, BlotGlyco, Tetrodotoxin (TTX), and Bicuculline to enhance their understanding and applications of Aminopyridines.
PubCompare.ai's cutting-edge tools, such as the Axopatch 200B amplifier and DP-311 system, can help take your Aminopyridines research to the next level by providing access to a wealth of information, streamlining experimental design, and improving the overall quality and reproducibility of your work.
Whether you're studying the fundamental properties of Aminopyridines or exploring their potential therapeutic uses, PubCompare.ai's AI-powered platform can be an invaluable resource for your research endeavors.