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Alkynes

Alkynes are a class of organic compounds containing a carbon-carbon triple bond.
They exhibit unique chemical reactivity and are widely used in organic synthesis, materials science, and other fields.
Discvoer how PubCompare.ai's AI-driven tools can help identify the best alkyne research protocols from literature, preprints, and patents to streamline your workflow and enhance your research effeciency and results.

Most cited protocols related to «Alkynes»

In Vitro Synthesis of COX-2 Inhibitors

To investigate the COX-2 isozyme templated synthesis, each 5-azido-pyraozle (5, 14, 27, and 31, 1 µl of 3 mM DMSO solution) and alkyne (6a–6f, 15a–15e, 1 µl of 20 mM DMSO solution) were pairwise mixed with human recombinant COX-2 isozyme (95 µl COX-2) in 1 µl of 1 M Tris-HCl, pH 8.0. The each reaction mixture was vortexed for 1 min, and then incubated at room temperature (For temperature dependency of COX-2 enzyme activity, see Supplementary Fig. 16). Final reagent concentrations were as follows: COX-2 (7 µM), azide (30 µM) alkyne (200 µM). After 3, 6, 9, 12, 15, 18, 21, and 24 h each sample was analyzed in triplicate by injecting (10 µl) into the LC/MS instrument with SIM mode (Water’s Micromass ZQTM 4000 LC−MS instrument, operating in the ESI-positive mode, equipped with a Water’s 2795 separation module). Calibration curve for hit compounds 18 and 21 is given in Supplementary Fig. 17. Summaries of all LC/MS data are presented in Supplementary Tables 3–7. Separations were performed in triplicate using a Kromasil 100-5-C18 (100 μm pore size, 5 μm particle size) reverse phase column (2.1 mm diameter × 50 mm length), preceded by a Kromasil 100-5-C18 2.1 × guard column. Separations were effected using a gradient MeCN/H₂O (0.05% trifluoroacetic acid (TFA))/MeOH in 40/30/30, v/v/v over 15 min at flow rate 0.25 ml min⁻¹. Operating parameters were as follows: capillary voltage = 3.5 kV; cone voltage = 20 V; source temperature = 140 °C; sesolvation temperature = 250 °C; cone nitrogen gas flow = 100 l h⁻¹; desolvation nitrogen gas flow = 550 l h⁻¹. The identities of triazole products (retention time of 6.73 min for 18), (retention time of 4.56 min for 21), and the internal standard (retention time of 10.89 min) were confirmed by molecular weight and comparison of the retention times of the authentic products formed from copper catalyzed reactions. Control experiments in the presence of BSA (1 mg mL⁻¹) instead of the COX-2 enzyme as well as in the absence of COX-2 enzyme and the known COX-2 selective inhibitor (1 µl of celecoxib, 100 µM final concentration) were run as described above. For multicomponent in situ click chemistry reactions, each azide (5, 14, 27, and 31, 1 µL of 3 mM DMSO solution) and eleven alkynes (6a–6f and 15a–15e, 1 µl of 20 mM DMSO solution) were thoroughly mixed together in the presence of COX-2 isozyme (95 µl COX-2) in 1 µl of 1 M Tris-HCl, pH 8.0 and incubated at room temperature. After 24 h each sample was analyzed in triplicate by injecting (10 µl) into the LC/MS instrument by following the procedure described above, except the ions are monitored for all possible masses. The cyclo addition products were identified by their molecular weights and by comparison of the retention times of authentic products prepared through Cu-catalyzed reactions. Control experiments using BSA (1 mg ml⁻¹) in place of COX-2 isozyme and in the absence of COX-2 isozyme were run consecutively.

Bhardwaj A., Kaur J., Wuest M, & Wuest F. (2017). In situ click chemistry generation of cyclooxygenase-2 inhibitors. Nature Communications, 8, 1.

Publication 2017

Alkynes Anabolism Azides Capillaries Celecoxib compound 18 Copper Cyclooxygenase 2 Inhibitors enzyme activity Enzymes Homo sapiens Ions Isoenzymes Nitrogen PTGS2 protein, human Retention (Psychology) Retinal Cone Sulfoxide, Dimethyl Triazoles Trifluoroacetic Acid Tromethamine

Measuring Protein Synthesis in Cells

For in vitro analysis 10³-10⁴ bone marrow or sorted cells were plated in 100 μl of methionine free Dulbecco’s Modified Eagle’s Medium (Sigma) supplemented with 200 μM L-cysteine (Sigma), 50 μM 2-mercaptoethanol (Sigma), 1mM L-glutamine (Gibco) and 0.1% bovine serum albumin (BSA; Sigma). For analysis of HPG and AHA incorporation, cells were pre-cultured for 45 minutes to deplete endogenous methionine. For OP-Puro, the medium was supplemented with 1mM L-methionine (Sigma). HPG (Life Technologies; 1mM final concentration), AHA (Life Technologies; 1mM final concentration) or OP-Puro (Medchem Source; 50 μM final concentration) were added to the culture medium for 1 hour (HPG and OP-Puro) or 2.5 hours (AHA), then cells were removed from wells and washed twice in Ca²⁺ and Mg²⁺ free phosphate buffered saline (PBS). Cells were fixed in 0.5ml of 1% paraformaldehyde (Affymetrix) in PBS for 15 minutes on ice. Cells were washed in PBS, then permeabilized in 200 μl PBS supplemented with 3% fetal bovine serum (Sigma) and 0.1% saponin (Sigma) for 5 minutes at room temperature. The azide-alkyne cycloaddition was performed using the Click-iT Cell Reaction Buffer Kit (Life Technologies) and azide conjugated to Alexa Fluor 488 or Alexa Fluor 555 (Life Technologies) at 5μM final concentration. After the 30 minute reaction, the cells were washed twice in PBS supplemented with 3% fetal bovine serum and 0.1% saponin, then resuspended in PBS supplemented with 4’,6-diamidino-2-phenylindole (DAPI; 4 μg/ml final concentration) and analyzed by flow cytometry. To inhibit OP-Puro, HPG or AHA incorporation, cycloheximide (Sigma) was added 30 minutes prior to OP-Puro or HPG at a final concentration of 100 μg/ml. All cultures were incubated at 37°C in 6.5% CO₂ and constant humidity.
For in vivo analysis, OP-Puro (50mg/kg body mass; pH 6.4–6.6 in PBS) was injected intraperitoneally. One hour later mice were euthanized, unless indicated otherwise. Bone marrow was harvested, and 3×10⁶ cells were stained with combinations of antibodies against cell surface markers as described below. After washing, the cells were fixed, permeabilized, and the azide-alkyne cycloaddition was performed as described above. “Relative rates of protein synthesis” were calculated by normalizing OP-Puro signals to whole bone marrow after subtracting autofluorescence background. “Mean OP-Puro fluorescence” reflected absolute fluorescence values for each cell population from multiple independent experiments.
To assess the effect of proteasome activity on OP-Puro incorporation mice were administered an intravenous injection of bortezomib (Cell Signaling; 1mg/kg body mass) 1 hour before OP-Puro administration. OP-Puro incorporation was assessed as described above 1 hour later unless indicated otherwise.

Signer R.A., Magee J.A., Salic A, & Morrison S.J. (2014). Haematopoietic stem cells require a highly regulated protein synthesis rate. Nature, 509(7498), 49-54.

Publication 2014

2-Mercaptoethanol alexa fluor 488 Alexa Fluor 555 Alkynes Antibodies Azides Bone Marrow Bortezomib Cardiac Arrest Cells Culture Media Cycloaddition Reaction Cycloheximide Cysteine DAPI Eagle Fetal Bovine Serum Flow Cytometry Fluorescence Glutamine Human Body Humidity Methionine Multicatalytic Endopeptidase Complex Mus O-propargyl-puromycin paraform Phosphates Protein Biosynthesis Saline Solution Saponin Serum Albumin, Bovine

Enantioselective Addition of TMS-acetylene to Cinnamaldehyde

Full experimental details can be found in the Supporting Information.
To a solution of (S,S)-ProPhenol ligand (20.8 mg, 0.0325 mmol, 10 mol%), triphenylphosphine oxide (18 mg, 0.065 mmol, 20 mol %) and TMS-acetylene (56 μL, 0.39 mmol, 1.2 equiv) in anhydrous toluene (0.44 mL) was added dimethyl zinc (406 μL, 1.2 M solution in toluene, 0.488 mmol, 1.5 equiv) at 0 °C (0.813 mL total toluene, 0.48 M alkyne concentration). The reaction was warmed to room temperature and stirred for 60 minutes before addition of the trans-cinammaldehyde (43 mg, 0.325 mmol, 1 equiv) at 0 °C. The reaction was stirred for 48 hours at 4 °C before quenching with saturated, aqueous NH₄Cl. The organic phase was extracted three times with Et₂O and the combined organics were concentrated in vacuo. The crude product was purified by flash column chromatography. The title compound was isolated as a white solid (67 mg, 83% yield). Melting Point: 57-58 °C. [α]_D25 = +2.16° (c = 1.05, CHCl₃). ¹H-NMR (400 MHz, CDCl₃): δ 7.40-7.43 (m, 2H), 7.32-7.36 (m, 2H), 7.25-7.29 (m, 1H), 6.77 (dd, J = 16, 1.2 Hz, 1H), 6.29 (dd, J = 16, 6 Hz, 1H), 5.05 (dt, J = 6, 1.2 Hz, 1H), 1.96 (t, J = 6 Hz, 1H), 0.21 (s, 9H). ¹³C-NMR (101 MHz, CDCl₃): δ 136.0, 132.0, 128.6, 128.1, 127.8, 126.8, 104.1, 91.3, 66.3, −0.2. IR (film): 3300 (br, OH), 2960, 2172, 1654, 1496, 1449, 1407, 1251 cm⁻¹. HRMS–EI (m/z): calculated for C₁₄H₁₈OSi: 230.1127, found: 230.1126, 0.6 ppm. Chiral HPLC: Chiralcel® AD column, heptane/iPrOH = 90/10, 1.0 mL/min, λ = 254 nm: 6.97/8.79 min (88% ee). Characterization data matches literature.^{[45 ]}

Trost B.M., Bartlett M.J., Weiss A.H., von Wangelin A.J, & Chan V.S. (2012). Development of Zn-ProPhenol-Catalyzed Asymmetric Alkyne Addition: Synthesis of Chiral Propargylic Alcohols. Chemistry (Weinheim an der Bergstrasse, Germany), 18(51), 10.1002/chem.201202085.

Publication 2012

1H NMR Acetylene Alkynes Carbon-13 Magnetic Resonance Spectroscopy Chloroform Chromatography Heptane High-Performance Liquid Chromatographies Ligands Toluene triphenylphosphine oxide Zinc

Profiling Proteome-wide Covalent Interactions

IsoTOP-ABPP studies were done as previously reported^{12 (link),14 (link),15 (link)}. Cells were lysed by probe sonication in PBS and protein concentrations were measured by BCA assay³⁵. For in situ experiments, cells were treated for 90 min with either DMSO vehicle or covalently-acting small molecule (from 1000× DMSO stock) before cell collection and lysis. Proteomes were subsequently labeled with IA-alkyne labeling (100 μM) for 1 h at room temperature. CuAAC was used by sequential addition of tris(2-carboxyethyl)phosphine (1 mM, Sigma), tris[(1-benzyl-1H-1,2,3-triazol-4-yl)methyl]amine (34 μM, Sigma), copper (II) sulfate (1 mM, Sigma), and biotin-linker-azide—the linker functionalized with a TEV protease recognition sequence as well as an isotopically light or heavy valine for treatment of control or treated proteome, respectively. After CuAAC, proteomes were precipitated by centrifugation at 6500 × g, washed in ice-cold methanol, combined in a 1:1 control/treated ratio, washed again, then denatured and resolubilized by heating in 1.2 % SDS/PBS to 80°C for 5 minutes. Insoluble components were precipitated by centrifugation at 6500 × g and soluble proteome was diluted in 5 ml 0.2% SDS/PBS. Labeled proteins were bound to avidin-agarose beads (170 μl resuspended beads/sample, Thermo Pierce) while rotating overnight at 4°C. Bead-linked proteins were enriched by washing three times each in PBS and water, then resuspended in 6 M urea/PBS (Sigma) and reduced in TCEP (1 mM, Sigma), alkylated with iodoacetamide (IA) (18 mM, Sigma), then washed and resuspended in 2 M urea and trypsinized overnight with 0.5 μg/μl sequencing grade trypsin (Promega). Tryptic peptides were eluted off. Beads were washed three times each in PBS and water, washed in TEV buffer solution (water, TEV buffer, 100 μM dithiothreitol) and resuspended in buffer with Ac-TEV protease and incubated overnight. Peptides were diluted in water and acidified with formic acid (1.2 M, Spectrum) and prepared for analysis.

Spradlin J.N., Hu X., Ward C.C., Brittain S.M., Jones M.D., Ou L., To M., Proudfoot A., Ornelas E., Woldegiorgis M., Olzmann J.A., Bussiere D.E., Thomas J.R., Tallarico J.A., McKenna J.M., Schirle M., Maimone T.J, & Nomura D.K. (2019). Harnessing the Anti-Cancer Natural Product Nimbolide for Targeted Protein Degradation. Nature chemical biology, 15(7), 747-755.

Publication 2019

Alkynes avidin-agarose Azides Biotin bropirimine Buffers Cells Centrifugation Cold Temperature Copper Dithiothreitol formic acid Iodoacetamide Light link protein Methanol methylamine Peptides phosphine Promega Proteins Proteome Sulfates, Inorganic Sulfoxide, Dimethyl TEV protease tris(2-carboxyethyl)phosphine Tromethamine Trypsin Urea Valine

Methionine and Homopropargylglycine Labeling in Cartilage

Samples were cultured in a chemically defined media: high glucose DMEM without glutamine, methionine, or cystine (Life Technologies 21013024) supplemented with either 0.1 mM L-methionine (Sigma M5308; control media) or 0.1 mM L-homopropargylglycine (Molecular Probes C10186; labeling media), 10 ng/ml TGFβ-3, 0.1 μM dexamethasone, 4 mM L-glutamine, 0.201 mM cystine (Sigma C7602), 100 μg/mL sodium pyruvate, 1.25 mg/mL bovine serum albumin, 0.1% ITS premix, 50 μg/mL ascorbate 2-phosphate, 40 μg/mL proline, and 1% penicillin-streptomycin-amphotericin. Medium was replenished every 2–3 days, and samples were finally fixed in 4% phosphate-buffered paraformaldehyde for 15 minutes before storage in PBS at 4 °C. Cartilage plugs (4 mm diameter) were cultured in labeling media for 3 days, and fixed in 4% PFA overnight.
HPG incorporated into fixed samples was covalently tagged with Alexa Fluor 488. Samples collected up to day 9 were stained and imaged as intact gels. To improve imaging, cartilage and gels collected at 21 and 42 days were cryosectioned to yield 40 μm thick cross-sections. Both intact gels and cryosections were first stained with a 1:1000 dilution of a plasma membrane stain (Molecular Probes C10046) in PBS for 30 minutes at room temperature. Next, samples were rinsed twice with PBS, and incubated in a click reaction labeling solution (prepared from Molecular Probes C10428 according to product instructions, and including Alexa Fluor 488 azide) for 40 minutes at room temperature. Samples were washed in reaction rinse buffer (Molecular Probes C10428, 5 minutes at room temperature), and then once with PBS. Nuclei were labeled with Hoechst in PBS for 15 minutes at room temperature, and samples were washed twice with PBS before imaging. The same labeling procedure was followed for AHA samples, with Alexa Fluor 594 alkyne (Molecular Probes C10102 and A10275).

McLeod C.M, & Mauck R.L. (2016). High fidelity visualization of cell-to-cell variation and temporal dynamics in nascent extracellular matrix formation. Scientific Reports, 6, 38852.

Publication 2016

Alexa594 alexa fluor 488 Alkynes Amphotericin ascorbate-2-phosphate Azides Buffers Cartilage Cell Nucleus Cryoultramicrotomy Culture Media Cystine Dexamethasone Gels Glucose Glutamine homopropargylglycine Methionine Molecular Probes paraform Penicillins Phosphates Plasma Membrane Proline Pyruvate Serum Albumin, Bovine Sodium Stains Streptomycin Technique, Dilution Transforming Growth Factor beta3

Most recents protocols related to «Alkynes»

Azide-Alkyne Click Conjugation of Polymer and DNA Oligo

Not available on PMC !

Example 47

Azide Polymer Synthesis for Click Conjugation to Alkyne Terminated DNA Oligo

A solution of azidohexanoic acid NHS ester (2.5 mg) in anhydrous DMF (100 μL) was added to a solution of the amine-functional polymer (9.9 mg) in anhydrous DMF (100 μL) under argon. Diisopropylethylamine (2 μL) was then added. The reaction was agitated at room temperature for 15 hours. Water was then added (0.8 mL) and the azide-modified polymer was purified over a NAP-10 column. The eluent was freeze dried overnight. Yield 9.4 mg, 95%.

Oligo Synthesis with Pendant Alkyne (Hexyne) for Click Conjugation to Azide Polymer

The 3′ propanol oligo A8885 (sequence YATTTTACCCTCTGAAGGCTCCP, where Y=hexynyl group and P=propanol group) was synthesized using 3′ spacer SynBase™ CPG 1000 column on an Applied Biosystems 394 automated DNA/RNA synthesizer. A standard 1.0 mole phosphoramidite cycle of acid-catalyzed detritylation, coupling, capping and iodine oxidation was used. The coupling time for the standards monomers was 40 s, and the coupling time for the 5′ alkyne monomer was 10 min.

The oligo was cleaved from the solid support and deprotected by exposure to concentrated aqueous ammonia for 60 min at room temperature, followed by heating in a sealed tube for 5 h at 55° C. The oligo was then purified by RP-HPLC under standard conditions. Yield 34 OD.

Solution Phase Click Conjugation: Probe Synthesis

A solution of degassed copper sulphate pentahydrate (0.063 mg) in aqueous sodium chloride (0.2 M, 2.5 μL) was added to a degassed solution of tris-benzo triazole ligand (0.5 mg) and sodium ascorbate (0.5 mg) in aqueous sodium chloride (0.2 M, 12.5 μL). Subsequently, a degassed solution of oligo A8885 (50 nmole) in aqueous sodium chloride (0.2 M, 30 μL) and a degassed solution of azide polymer (4.5 mg) in anhydrous DMF (50 μL) were added, respectively. The reaction was degassed once more with argon for 30 s prior to sealing the tube and incubating at 55° C. for 2 h. Water (0.9 mL) was then added and the modified oligo was purified over a NAP-10 column. The eluent was freeze-dried overnight. The conjugate was isolated as a distinct band using PAGE purification and characterized by mass spectrometry. Yield estimated at 10-20%.

Fluorescence Studies

The oligo-polymer conjugate was used as a probe in fluorescence studies. The probe was hybridized with the target A8090 (sequence GGAGCCTTCAGAGGGTAAAAT-Dabcyl), which was labeled with dabcyl at the 3′ end to act as a fluorescence quencher. The target and probe were hybridized, and fluorescence monitored in a Peltier-controlled variable temperature fluorimeter. The fluorescence was scanned every 5° C. over a temperature range of 30° C. to 80° C. at a rate of 2° C./min. FIG. 25 shows increasing fluorescence intensity or emission with increasing temperature, indicating that as the probe-target pair melt, the polymer and quencher separate and fluorescence is recovered.

Polymer conjugation to nucleic acids can also be performed using methods adapted from the protocols described in Examples 14, 45 and 46.

US11874278B2. Reagents for directed biomarker signal amplification (2024-01-16). SIRIGEN II LIMITED [GB]. Inventors: Brent S. Gaylord [US], Glenn P. Bartholomew [US], Russell A. Baldocchi [US], Janice W. Hong [US], William H. Huisman [US], Yongchao Liang [US], Trung Nguyen [US], Lan T. Tran [US], Jean M. Wheeler [US], Adrian Charles Vernon Palmer [GB], Frank Peter Uckert [US].

Patent 2024

4-(4-dimethylaminophenylazo)benzoic acid Acids Alkynes Amines Ammonia Anabolism Argon Azides DNA Replication Esters Fluorescence Freezing High-Performance Liquid Chromatographies Iodine Ligands Mass Spectrometry Moles Nucleic Acids Oligonucleotides phosphoramidite Polymers Propanols Sodium Ascorbate Sodium Chloride Spacer DNA Sulfate, Copper Triazoles Tromethamine

DFT Study of Alkyne Hydrothiolation Reactions

The computational study was performed by using the ORCA software package.²⁶ The density functional theory (DFT)²⁷ energies were obtained with the PBE0 functional,²⁸ applying the D3BJ Grimme's dispersion correction,^{29 (link)} which is known to be an appropriate methodology for similar mechanistic studies on alkyne hydrothiolation reactions²² as well as for the modelling of copper complexes,^{30 (link)} and the triple-ζ def2-TZVP basis set³¹ for all atoms. The energies in solution were obtained with the conductor-like polarizable continuum model (CPCM)³² using dichloromethane (DCM) as provided by the library of solvents of ORCA v. 4.2.1.

Capurso M., Radivoy G., Nador F, & Dorn V. (2023). Hydrothiolation of alkynes with thiol–catechol derivatives catalysed by CuNPs/TiO2: exploring the reaction mechanism by DFT calculations. RSC Advances, 13(12), 8025-8033.

Publication 2023

Alkynes cDNA Library Copper Methylene Chloride Orcinus orca Solvents

Glycoproteome Profiling in MCF7 Cells

MCF7 cells (from the American Type Culture Collection, ATCC) were
grown in DMEM medium (Sigma-Aldrich) containing 10% fetal bovine serum
(FBS, Thermo) at 37 °C with 5.0% CO₂ in a humidified
incubator. When the confluency reached 80%, the medium was replaced
using a heavy lysine (K8) and arginine (R6) containing medium, and
250 μM N-azidoacetylgalactosamine-tetraacetylated
(Ac₄GalNAz, Click Chemistry Tools) and 50 μM puromycin
(Puro, Santa Cruz Biotechnology) were added to the medium. For the
control samples, Puro was not added. Then, cells were treated for
1 h. For the boosting sample, cells were cultured in the medium containing
heavy lysine and arginine for 2 weeks for complete labeling of proteins
with heavy K and R in the cells. Then the cells were treated with
250 μM Ac₄GalNAz for 48 h to label O-GlcNAcylated proteins.
Cells from different samples were harvested
and washed with ice-cold PBS twice. They were lysed with a buffer
containing 50 mM HEPES, pH = 7.4, 150 mM NaCl, 0.5% SDC, 0.1% SDS,
1% NP-40, 50 μM Thiamet G, 50 units/mL Benzonase nuclease (Millipore),
and 1 tablet/10 mL EDTA-free protease inhibitor for 2 h at 4 °C.
Then the lysates were centrifuged for 10 min at 4696g, and the debris was discarded. The labeled glycopeptides or glycoproteins
were reacted with a biotin probe through a click chemistry reaction.
In the cell lysate, 250 μM photocleavable (PC) biotin-alkyne
(Click Chemistry Tools), 1 mM CuSO₄, 5 mM Tris(3-hydroxypropyltriazolylmethyl)
amine (THPTA, Click Chemistry Tools), 5% dimethyl sulfoxide (DMSO),
15 mM sodium l-ascorbate (Sigma), and 15 mM aminoguanidine
hydrochloride (Sigma) were added, and the reaction lasted for 2 h
at room temperature.

Xu S., Yin K, & Wu R. (2023). Combining Selective Enrichment and a Boosting Approach to Globally and Site-Specifically Characterize Protein Co-translational O-GlcNAcylation. Analytical Chemistry, 95(9), 4371-4380.

Publication 2023

Alkynes Amines Arginine Benzonase Biotin Cells Cold Temperature Culture Media Edetic Acid Glycopeptides HEPES Lysine MCF-7 Cells Nonidet P-40 Proteins Puromycin SERPINA1 protein, human Sodium Ascorbate Sodium Chloride Somatostatin-Secreting Cells Sulfoxide, Dimethyl Tablet thiamet G Tromethamine

Copper-Catalyzed Alkyne-Aryl Halide Coupling

Substituted aryl halides (0.25 mmol, 1 eq.) and terminal alkynes (0.3 mmol, 1.2 eq.) were added to a mixture of water : ethanol (4 mL) and placed in 10 mL Monowave 50 vial. After adding potassium carbonate (0.75 mmol, 3 eq.) and catalyst 3 (7.50 mg, 5.0 μmol, 2 mol%), the reaction mixture was heated at 120 °C for 20 minutes (or the time indicated in Table 4) in Monowave 50 heating reactor in a sealed vial. Upon the completion of the reaction, the mixture was extracted with dichloromethane (2 × 5 mL). The organic layers were combined, dried over sodium sulfate, and filtered. The solvent was removed in vacuo and the final products was purified by flash chromatography on silica gel using hexane: ethyl acetate as the eluent.

Wilson K.A., Picinich L.A, & Siamaki A.R. (2023). Nickel–palladium bimetallic nanoparticles supported on multi-walled carbon nanotubes; versatile catalyst for Sonogashira cross-coupling reactions. RSC Advances, 13(12), 7818-7827.

Publication 2023

Alkynes Chromatography Ethanol ethyl acetate Methylene Chloride n-hexane potassium carbonate Silica Gel sodium sulfate Solvents

Sonogashira Cross-Coupling Reactions with MWCNTs

Nickel(ii) acetate tetrahydrate and palladium acetate were obtained from Sigma-Aldrich. Aryl iodides and bromides, and functionalized terminal alkynes were purchased from MilliporeSigma, Alfa Aesar, and ACROS Organics and used as received. Multi-walled carbon nanotubes (MWCNTs) 50–85 nm was purchased from Graphene Supermarket. A mixture of ethanol–deionized water was used as the solvent system for all the reactions. Transmission electron microscopy was performed on ThermoFisher Talos F200X G2, a 200 kV FEG (Field Emission Gun) Analytical Scanning Transmission Electron Microscope (S/TEM). X-ray diffraction (XRD) was accomplished on Rigaku MiniFlex 600 X-ray diffractometer. X-ray photoelectron spectroscopy (XPS) was performed on Kratos Axis Supra X-ray photoelectron spectrometer. Inductively Coupled Plasma-Mass Spectrometry (ICP-MS) analysis was completed using NexION 300D (PerkinElmer, Inc.). Gas Chromatography-Mass Spectroscopy (GC-MS) of organic products was analyzed using a Shimadzu GC-MS QP2010 SE. ¹H and ¹³C NMR spectra were acquired on a JEOL 400 MHz spectrometer equipped with autosampler. All Sonogashira cross-coupling reactions were performed using Anton-Paar Monowave 50 heating reactor.

Publication 2023

Acetate Alkynes Bromides Carbon-13 Magnetic Resonance Spectroscopy Cross Reactions Epistropheus Ethanol Gas Chromatography-Mass Spectrometry Graphene Iodides Mass Spectrometry Nanotubes, Carbon Nickel Palladium Plasma Radiography Scanning Transmission Electron Microscopy Solvents Transmission Electron Microscopy X-Ray Diffraction

Top products related to «Alkynes»

Click it protein reaction buffer kit by Thermo Fisher Scientific

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The Click-iT Protein Reaction Buffer Kit is a set of reagents designed to enable the detection and analysis of newly synthesized proteins in cells. The kit provides the necessary components to facilitate the incorporation of a modified amino acid, which can then be detected using a click chemistry reaction.

Click it cell reaction buffer kit by Thermo Fisher Scientific

Sourced in United States, Germany

The Click-iT Cell Reaction Buffer Kit is a laboratory tool designed to facilitate the detection and analysis of cellular processes. It provides the necessary components to perform click chemistry reactions within cells, enabling the labeling and visualization of specific biomolecules or cellular events.

Biotin alkyne by Thermo Fisher Scientific

Sourced in United States

Biotin-alkyne is a small-molecule labeling reagent used in various biochemical and cell biology applications. It consists of a biotin moiety and an alkyne functional group, which allows for selective labeling and detection of biomolecules, such as proteins, glycans, or lipids, that have been modified to contain azide groups.

Cuso4 by Merck Group

Sourced in United States, Germany, China, Macao, United Kingdom, Italy, Switzerland

CuSO4 is a chemical compound composed of copper (Cu) and sulfate (SO4). It is a blue crystalline solid that is widely used in various industrial and laboratory applications. The core function of CuSO4 is to serve as a source of copper ions, which can be utilized in a variety of chemical processes and analyses.

Sodium ascorbate by Merck Group

Sourced in United States, Germany, France, United Kingdom

Sodium ascorbate is a water-soluble salt of ascorbic acid (vitamin C). It serves as a source of vitamin C for various laboratory and research applications.

Alexa fluor 488 alkyne by Thermo Fisher Scientific

Alexa Fluor 488 Alkyne is a fluorescent dye used in molecular biology and biochemistry applications. It is a member of the Alexa Fluor dye series and has an excitation maximum at 488 nm and an emission maximum at 515 nm. The alkyne functional group allows for bioconjugation to biomolecules, such as proteins and nucleic acids.

L azidohomoalanine aha by Thermo Fisher Scientific

Sourced in United States

L-azidohomoalanine (AHA) is a non-canonical amino acid that can be used as a metabolic label for the detection and identification of newly synthesized proteins. AHA is structurally similar to the natural amino acid methionine and can be incorporated into proteins during translation.

Thpta by Merck Group

Sourced in United States

THPTA is a chemical compound used in laboratory settings. It is a tris(hydroxypropyl)phosphine oxide that serves as a ligand in various chemical reactions and processes. The core function of THPTA is to facilitate and stabilize metal-ligand complexes, which are essential for numerous applications in analytical and synthetic chemistry.

5 bromo 1 pentyne by Merck Group

5-bromo-1-pentyne is a chemical compound used in various laboratory applications. It is a halogenated alkyne that can be used as a building block or a precursor in organic synthesis and other chemical reactions. The core function of this product is to serve as a versatile reagent for chemical transformations and modifications in a laboratory setting.

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What are the unique properties and reactivity of Alkynes?

Alkynes are a class of organic compounds containing a carbon-carbon triple bond. This triple bond confers unique chemical reactivity, such as high polarizability and the ability to undergo various addition reactions. The carbon-carbon triple bond also makes alkynes more rigid and linear compared to alkanes and alkenes. These properties make alkynes valuable in organic synthesis, materials science, and other fields where their distinctive reactivty is leveraged.

What are some common applications of Alkynes?

Alkynes have a wide range of applications due to their distinctive reactivity and structural properties. They are widely used as building blocks in organic synthesis, particularly in the construction of complex molecules. Alkynes are also employed in the synthesis of polymeric materials, with their triple bonds allowing for crosslinking and the creation of robust, functional materials. Additionally, alkynes find use in the pharmaceutical industry, where they can be incorporated into drug molecules to modulate their pharmacological properties.

How can PubCompare.ai help researchers working with Alkynes?

PubCompare.ai's AI-driven tools can greatly assist researchers working with alkynes by helping them identify the most effective and reproducible research protocols from the literature, preprints, and patents. The platfrom's analysis can highlight key differences in protocol effectiveness, enabling researchers to choose the best option for their specific goals. This streamlines the research workflow and enhances efficiency, allowing researchers to focus on generating high-quality results rather than spending time sifting through a vast amount of information.

What are some common challenges in working with Alkynes, and how can PubCompare.ai help address them?

One of the main challenges in working with alkynes is the need to ensure high levels of reproducibility and accuracy in experimental protocols. Alkynes can be sensitive to reaction conditions, and slight variations in parameters can significantly impact the outcome. PubCompare.ai's AI-driven analysis can help researchers identify the most robust and reliable protocols, allowing them to avoid pitfalls and achieve consistent, high-quality results. The platform's side-by-side comparison of protocols can also reveal critical insights that may not be apparent from individual studies, guiding researchers to the optimal approach for their specific research goals.

Are there different types or variations of Alkynes, and how do they differ?

Yes, there are several different types and variations of alkynes. For example, terminal alkynes have the triple bond at the end of the carbon chain, while internal alkynes have the triple bond within the chain. Speciality alkynes, such as fluorinated or cyclic alkynes, also exist and exhibit unique properties. The choice of alkyne type can have a significant impact on the outcome of synthetic reactions or material properties. PubCompare.ai's platform can help researchers compare the performance of different alkyne variations, allowing them to select the most appropriate option for their specific application.

More about "Alkynes"

Alkynes are a class of organic compounds characterized by the presence of a carbon-carbon triple bond.
These versatile molecules exhibit unique chemical reactivity and are widely utilized in various fields, including organic synthesis, materials science, and beyond.
Alkyne-containing compounds are often employed in click chemistry reactions, such as the copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction.
This powerful tool allows for the selective and efficient conjugation of biomolecules, including proteins, using reagents like the Click-iT Protein Reaction Buffer Kit and Click-iT Cell Reaction Buffer Kit.
Biotin-alkyne is another commonly used alkyne-bearing compound that enables the labeling and detection of biomolecules.
The CuAAC reaction requires the use of copper(II) sulfate (CuSO4) as a catalyst, which is often used in conjunction with the reducing agent sodium ascorbate to generate the active copper(I) species.
Fluorescent dyes, such as Alexa Fluor 488 Alkyne, can be incorporated into alkyne-containing structures, enabling visualization and tracking of labeled biomolecules.
Alkynes can also be used to metabolically label proteins with non-canonical amino acids, like L-azidohomoalanine (AHA), which can then be detected through click chemistry reactions.
The tris(3-hydroxypropyltriazolylmethyl)amine (THPTA) ligand is often employed to enhance the efficiency and selectivity of these reactions.
In addition to their applications in chemical biology, alkynes find use in the synthesis of various compounds, including 5-bromo-1-pentyne, which can serve as a building block for more complex molecular structures.
The versatility of alkynes is further demonstrated by their utility in diverse analytical techniques, such as the ChemiDoc MP Imaging System, which can detect and quantify alkyne-labeled biomolecules.
Whether you're working in organic synthesis, materials science, or exploring the intricacies of biomolecular interactions, understanding the unique properties and applications of alkynes can be a valuable asset in your research endeavors.
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