The detailed synthesis of p-FTAA, p-FTAM and p-FTAA are shown in the supplementary material and in scheme 1 . Briefly, all of the LCO were synthesized by iodination of a trimeric thiophene precursor (1 ) (15 (link)). The iodinated trimer (2 ) was further converted to pentamers by addition of 2-thiopheneboronic acid or 5-(dihydroxyboryl)-2-thiophenecarboxylic through Suzuki coupling (3 , p-FTAM (5 )). The methyl group was removed by NaOH to achieve p-HTAA (4 ) and p-FTAA (6 ). p-HTAA and p-FTAA was converted to its corresponding sodium salt by dissolving it in H2O and equimolar amounts of sodium hydroxide, relative the number of carboxylic acids.
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Phenomena
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Natural Phenomenon or Process
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Iodination
Iodination
Iodination is a chemical process that involves the introduction of iodine atoms into organic compounds, often used in scientific research and medical applications.
This technique is employed to label molecules with radioactive iodine isotopes for imaging and diagnostic purposes, as well as to modify the chemical and physical properties of compounds.
Iodination plays a crucial role in a variety of fields, including biochemistry, pharmacology, and materials science.
Researchers can streamline their iodination protocols and enhance reproducibility using PubComapre.ai's AI-driven platform, which helps identify the best procedures and products from literature, preprints, and patents.
This technique is employed to label molecules with radioactive iodine isotopes for imaging and diagnostic purposes, as well as to modify the chemical and physical properties of compounds.
Iodination plays a crucial role in a variety of fields, including biochemistry, pharmacology, and materials science.
Researchers can streamline their iodination protocols and enhance reproducibility using PubComapre.ai's AI-driven platform, which helps identify the best procedures and products from literature, preprints, and patents.
Most cited protocols related to «Iodination»
Acids
Anabolism
Carboxylic Acids
Iodination
pentamer formyl thiophene acetic acid
Sodium
Sodium Chloride
Sodium Hydroxide
Thiophene
Antibodies
Antibodies, Anti-Idiotypic
Biological Assay
Carbohydrates
Dietary Supplements
Digestion
Iodination
Mass Spectrometry
Oligosaccharides
Protein Subunits
Radioligand Assay
Angiotensin I
angiotensin I (1-7)
ANGPT1 protein, human
chloramine-T
High-Performance Liquid Chromatographies
Iodination
Metabolism
Oxidants
Peptides
sodium bisulfate
ELISA was performed as an in vitro quality control in order to assess the potential effect of radiolabelling on mAb3D6-scFv8D3 and di-scFv3D6-8D3. Indirect ELISA was used to measure mAb3D6-scFv8D3 and di-scFv3D6-8D3 binding to Aβ42 before and after 125I-iodination, as described previously [4 (link)]. For murine TfR1 (mTfR1) binding before and after radiolabelling, indirect ELISA was used for mAb3D6-scFv8D3 and a competition ELISA was used for di-scFv3D6-8D3 [6 (link)]. All of the ELISA setups are described in more detail in the Additional file 1 : Figs. S2 and S3.
Enzyme-Linked Immunosorbent Assay
Figs
Iodination
Mus
TFRC protein, human
Dichlorodiphenyldichloroethane
Exosomes
Iodination
Normal Saline
Tissue, Membrane
Most recents protocols related to «Iodination»
Example 5
Using N-succinimidyl-3-(4-hydroxy-3-[125I]iodophenyl)propionate, Bolton-Hunter Reagent (NEX120, PerkinElmer), the purified ST03-Cupid protein was radio-iodinated. Specifically, Bolton-Hunter Reagent in an amount of 20 times the number of moles of the used protein was taken in an Eppendorf tube, the solvent was then vaporized, and the protein solution was then added thereto. The mixture was reacted on ice for 2 hours. Thereafter, the reaction mixture was subjected to a desalination column (PD MiniTrap G-25, GE Healthcare) to remove unreacted radio-iodination Bolton-Hunter Reagent, and the resultant was then subjected to an ultrafiltration column (VIVASPIN Turbo 4, Sartorius) for concentration. After completion of the concentration, the amount of radioactivity was measured using a dose calibrator (CRC-25w, CAPINTEC), and the quality of the protein was checked by performing CBB staining according to SDS-PAGE.
Bolton-Hunter reagent
Iodination
Nevus
Propionate
Proteins
Radioactivity
SDS-PAGE
Solvents
Ultrafiltration
Prior to derivatization, acceptor solution was added to the extracted sample until a final volume of 100 µL was reached to have constant starting volumes for derivatization and ensure comparability between samples.
The samples were derivatized following a procedure based on a diazotization and subsequent iodination reactions [16 (link)]. Into 100 μL of the extracted sample, 100 μL hydriodic acid (55%) and 200 μL sodium nitrite (50 g/L) were added and the samples were shaken for 20 min at 300 rpm, transforming the amine group of the aromatic amines into diazonium ions. To destroy the surplus of nitrite, 500 μL of sulfamic acid (50 g/L) was added, shaking subsequently for 45 min at 300 rpm. The samples were then heated in a water bath at 95 °C for 5 min to facilitate the substitution of the diazo group by iodine. To reduce the surplus of iodine, 250 µL of sodium sulfite (120 g/L) was added to the cooled down sample, which triggered an immediate discoloration of the initially brownish solution. Finally, 100 μL of alizarin red S (1% w/v) and 92 µL NaOH (10 M) were added to the samples to adjust the pH of the sample to 5.
The samples used for the optimization tests were derivatized automatically thanks to the PAL RTC from CTC Analytics AG (Zwingen, Switzerland). A few modifications were done to the procedure, such as vortexing the reagents before addition and the samples after reagent addition. For the method validation experiments, the derivatization was done manually due to the increased throughput needed, since with the PAL RTC only six samples could be derivatized at the same time, due to the six positions in the agitator.
The samples were derivatized following a procedure based on a diazotization and subsequent iodination reactions [16 (link)]. Into 100 μL of the extracted sample, 100 μL hydriodic acid (55%) and 200 μL sodium nitrite (50 g/L) were added and the samples were shaken for 20 min at 300 rpm, transforming the amine group of the aromatic amines into diazonium ions. To destroy the surplus of nitrite, 500 μL of sulfamic acid (50 g/L) was added, shaking subsequently for 45 min at 300 rpm. The samples were then heated in a water bath at 95 °C for 5 min to facilitate the substitution of the diazo group by iodine. To reduce the surplus of iodine, 250 µL of sodium sulfite (120 g/L) was added to the cooled down sample, which triggered an immediate discoloration of the initially brownish solution. Finally, 100 μL of alizarin red S (1% w/v) and 92 µL NaOH (10 M) were added to the samples to adjust the pH of the sample to 5.
The samples used for the optimization tests were derivatized automatically thanks to the PAL RTC from CTC Analytics AG (Zwingen, Switzerland). A few modifications were done to the procedure, such as vortexing the reagents before addition and the samples after reagent addition. For the method validation experiments, the derivatization was done manually due to the increased throughput needed, since with the PAL RTC only six samples could be derivatized at the same time, due to the six positions in the agitator.
Alizarin Red S
Amines
Bath
hydroiodic acid
Iodination
Iodine
Ions
Nitrites
Sodium Nitrite
sodium sulfite
sulfamic acid
β-endorphin
was iodinated via reaction with NaI, chloramine-T, and sodium metabisulfite
in a manner to prevent excess iodination. Briefly, NaI and chloramine
T were combined in a 1:2 molar ratio prior to addition to β-endorphin.
Following this, 1/3 mol equiv of NaI:chloramine-T was added to 20
μL of 1 mM β-endorphin in water and allowed to react for
3 min before addition of the next equivalent for a total of 1 mol
equiv of NaI at 9 min. The reaction was then quenched with 4×
molar equivalents of sodium metabisulfite. A 20 μL aliquot of
1 mM RRLIEDNEYTARG was iodinated by reaction of peptide, NaI, and
chloramine T at a 1:1:2 molar ratio for 10 min. At 10 min, the reaction
was quenched by the addition of 4× molar equivalents of sodium
metabisulfite. AKAKTDHGAEIVYK was covalently modified with 4-iodobenzoic
acid (4IB) via reaction with 4IB-N hydroxy succinimide (4IB-NHS).
Briefly, 4IB-NHS was synthesized by reaction of 1:1:1 4IB:DCC:NHS
(0.5 mmol ea.) in 15 mL of dioxane for 12 h under N2. After
12 h, the reaction precipitate was removed via filtration, and dioxane
was gently evaporated with N2. Following this, covalent
attachment of 4IB was achieved by reaction of 50 μg of AKAKTDHGAEIVYK
in 25 μL of 100 mM borate buffer (pH 8.5) with 25 μL of
6.5 mM 4IB-NHS (10-fold molar excess) in dioxanes for 1 h. Iodo-RRLIEDNEYTARG
and 4IB-AKAKTDHGAEIVYK were desalted on a MICHROM Bioresources peptide
MicroTrap (P/N TR1/25109/02) directly following iodination to remove
salts and reaction byproducts prior to MS analysis. Following iodination,
iodo-β-endorphin was desalted on a MICHROM Bioresources protein
MicroTrap (P/N TR1/25109/03).
was iodinated via reaction with NaI, chloramine-T, and sodium metabisulfite
in a manner to prevent excess iodination. Briefly, NaI and chloramine
T were combined in a 1:2 molar ratio prior to addition to β-endorphin.
Following this, 1/3 mol equiv of NaI:chloramine-T was added to 20
μL of 1 mM β-endorphin in water and allowed to react for
3 min before addition of the next equivalent for a total of 1 mol
equiv of NaI at 9 min. The reaction was then quenched with 4×
molar equivalents of sodium metabisulfite. A 20 μL aliquot of
1 mM RRLIEDNEYTARG was iodinated by reaction of peptide, NaI, and
chloramine T at a 1:1:2 molar ratio for 10 min. At 10 min, the reaction
was quenched by the addition of 4× molar equivalents of sodium
metabisulfite. AKAKTDHGAEIVYK was covalently modified with 4-iodobenzoic
acid (4IB) via reaction with 4IB-N hydroxy succinimide (4IB-NHS).
Briefly, 4IB-NHS was synthesized by reaction of 1:1:1 4IB:DCC:NHS
(0.5 mmol ea.) in 15 mL of dioxane for 12 h under N2. After
12 h, the reaction precipitate was removed via filtration, and dioxane
was gently evaporated with N2. Following this, covalent
attachment of 4IB was achieved by reaction of 50 μg of AKAKTDHGAEIVYK
in 25 μL of 100 mM borate buffer (pH 8.5) with 25 μL of
6.5 mM 4IB-NHS (10-fold molar excess) in dioxanes for 1 h. Iodo-RRLIEDNEYTARG
and 4IB-AKAKTDHGAEIVYK were desalted on a MICHROM Bioresources peptide
MicroTrap (P/N TR1/25109/02) directly following iodination to remove
salts and reaction byproducts prior to MS analysis. Following iodination,
iodo-β-endorphin was desalted on a MICHROM Bioresources protein
MicroTrap (P/N TR1/25109/03).
beta-Endorphin
Borates
Buffers
chloramine-T
dioxane
Dioxanes
Filtration
Iodination
Iodine
Molar
Peptides
Sodium
sodium metabisulfite
Succinimides
8,9,12-I3-ortho-C2B10H9 was isolated as a by-product from the di-iodination reaction of ortho-carborane under standard conditions [51 (link)]. Iodine (3.553 g, 14.00 mmol) and anhydrous AlCl3 (0.400 g) were added to a solution of ortho-carborane (1.009 g, 7.00 mmol) in dichloromethane (30 mL) and heated under reflux for 8 h. Then, the reaction mixture was cooled and treated with a solution of Na2S2O3·5H2O (3.000 g) in water (50 mL). The organic phase was separated, and the aqueous fraction was extracted with dichloromethane (3 × 50 mL). The organic phases were combined, dried over Na2SO4, filtered, and concentrated under reduced pressure. The crude product was purified by column chromatography on silica using diethyl ether as eluent to yield 1.900 g (69%) of 9,12-I2-1,2-C2B10H10 and 0.102 g (3%) of 8,9,12-I3-1,2-C2B10H9 as white powders.
8,9,12-I3-1,2-C2B10H9: 1H NMR (CDCl3, ppm): 4.13 (2H, br s, CHcarb), 3.8−2.0 (7H, br m, BH). 11B NMR (CDCl3, ppm): δ −6.1 (1B, d, J = 157 Hz), −11.5 (4B, s + d), −13.1 (2B, d, J = 171 Hz), −14.7 (1B, d, J = 220 Hz), −16.4 (1B, d, J = 220 Hz), and −17.2 (1B, s, B(8)).
8,9,12-I3-1,2-C2B10H9: 1H NMR (CDCl3, ppm): 4.13 (2H, br s, CHcarb), 3.8−2.0 (7H, br m, BH). 11B NMR (CDCl3, ppm): δ −6.1 (1B, d, J = 157 Hz), −11.5 (4B, s + d), −13.1 (2B, d, J = 171 Hz), −14.7 (1B, d, J = 220 Hz), −16.4 (1B, d, J = 220 Hz), and −17.2 (1B, s, B(8)).
1H NMR
Aluminum Chloride
Chromatography
Ethyl Ether
Iodination
Methylene Chloride
Powder
Pressure
Silicon Dioxide
Direct iodination was investigated
with four oxidizing agents at pH 5 and pH 10. NMS (0.5 mg, 0.13 μmol)
was dissolved in 0.5 mL of PBS (pH 5 or pH 10) in a 1.5 mL LoBind
Eppendorf tube. Fifty nine micrograms (0.40 μmol, 3 equiv) of
sodium iodide, dissolved in 3.7 μL of PBS at pH 7.3, was added.
Four equivalents (0.53 μmol) of oxidation agents chloramine-T
(0.12 μg in 8.5 μL of PBS at pH 7.3), iodogen (0.23 μg
in 11.8 μL of PBS at pH 7.3), and freshly prepared chloramine
according to a published procedure24 (link) was
added. When using polymer-bound chloramine-T (loading: 0.2 mmol/g),
a single bead with a weight of 15 mg was used, which corresponds to
an amount of substance of about 3 μmol (22.7 equiv). The eight
samples were shaken at 22 °C by a horizontal rotation of 600
rpm. After 1 h, the samples were analyzed for their incorporation
of iodine by mass spectrometry.
with four oxidizing agents at pH 5 and pH 10. NMS (0.5 mg, 0.13 μmol)
was dissolved in 0.5 mL of PBS (pH 5 or pH 10) in a 1.5 mL LoBind
Eppendorf tube. Fifty nine micrograms (0.40 μmol, 3 equiv) of
sodium iodide, dissolved in 3.7 μL of PBS at pH 7.3, was added.
Four equivalents (0.53 μmol) of oxidation agents chloramine-T
(0.12 μg in 8.5 μL of PBS at pH 7.3), iodogen (0.23 μg
in 11.8 μL of PBS at pH 7.3), and freshly prepared chloramine
according to a published procedure24 (link) was
added. When using polymer-bound chloramine-T (loading: 0.2 mmol/g),
a single bead with a weight of 15 mg was used, which corresponds to
an amount of substance of about 3 μmol (22.7 equiv). The eight
samples were shaken at 22 °C by a horizontal rotation of 600
rpm. After 1 h, the samples were analyzed for their incorporation
of iodine by mass spectrometry.
chloramine-T
Iodides
Iodination
Iodine
Iodo-Gen
Mass Spectrometry
Oxidants
Polymers
Top products related to «Iodination»
Sourced in United States
The Pierce Pre-Coated Iodination Tubes are laboratory equipment designed for the iodination of proteins. The tubes are pre-coated with iodinating reagents, facilitating the iodination process and providing a convenient solution for researchers.
Sourced in United States
Na125I is a radioactive isotope of sodium that is used as a tracer in various laboratory applications. It emits gamma radiation, which can be detected and measured to provide information about the behavior and distribution of the labeled compounds or samples.
Sourced in United States, Sweden, Japan
Pierce Iodination Beads are a solid-phase iodination reagent designed for the labeling of proteins and other biomolecules with radioactive iodine. The beads contain immobilized lactoperoxidase, which catalyzes the iodination reaction.
The Pierce Iodination Reagent is a chemical used in the process of iodination, which is a common laboratory technique. It provides a stable and efficient way to introduce radioactive iodine isotopes into various biomolecules, such as proteins and peptides, for subsequent analysis or labeling purposes. The reagent enables the incorporation of iodine atoms into target analytes, facilitating their detection and quantification in various analytical methods.
Sourced in United States
Pre-coated Iodination tubes are laboratory equipment designed for the iodination of proteins, peptides, and other biomolecules. These tubes are pre-coated with a specialized reagent, facilitating the efficient and controlled iodination process.
Sourced in United States
[125I]NaI is a radioactive isotope of iodine that is used in various laboratory applications. It has a half-life of approximately 59 days and emits gamma radiation. [125I]NaI can be used as a tracer in biochemical and medical research.
Sourced in United States
The Pierce™ Iodination Tubes are laboratory equipment designed for the iodination of proteins. They provide a convenient and controlled environment for the radioactive labeling of proteins using iodine isotopes.
The Quick Spin Protein Columns are a type of lab equipment designed for rapid purification and concentration of proteins from samples. The columns utilize a centrifugation-based process to separate proteins from other components in the sample. This allows for quick and efficient protein extraction and preparation for further analysis or applications.
Sourced in United States
The 125I stock solution is a radioactive isotope of iodine used for various research and analytical applications in laboratories. It provides a consistent and reliable source of radioactivity for experiments and analyses requiring the use of a radioactive tracer.
Sourced in United States, United Kingdom, Germany, Sweden, Japan, Canada, Belgium
The PD-10 column is a size-exclusion chromatography column designed for desalting and buffer exchange of protein samples. It is commonly used to separate low molecular weight substances from high molecular weight compounds, such as proteins, in a rapid and efficient manner.
More about "Iodination"
Iodination is a crucial chemical process that involves the introduction of iodine atoms into organic compounds.
This versatile technique is widely employed in scientific research and medical applications.
Radiolabeling with radioactive iodine isotopes, such as 125I, is a common practice used for imaging, diagnostics, and modifying the properties of compounds.
Iodination plays a pivotal role in various fields, including biochemistry, pharmacology, and materials science.
To streamline iodination protocols and enhance reproducibility, researchers can leverage PubCompare.ai's AI-driven platform.
This cutting-edge technology helps identify the best procedures and products from literature, preprints, and patents.
By utilizing AI-driven comparisons, researchers can optimize their iodination workflows and improve experimental outcomes.
The iodination process can be facilitated using a range of specialized products, such as Pierce Pre-Coated Iodination Tubes, Na125I, Pierce Iodination Beads, and Pierce Iodination Reagent.
Pre-coated iodination tubes and [125I]NaI provide convenient options for radiolabeling, while Pierce™ Iodination Tubes and Quick Spin Protein Columns can be used to purify and isolate iodinated compounds.
The availability of 125I stock solution and PD-10 columns further enhances the versatility of iodination research.
PubCompare.ai's AI-driven platform is a valuable resource for researchers looking to optimize their iodination protocols and streamline their experimental processes.
By leveraging this cutting-edge technology, scientists can enhance the reproducibility and efficacy of their iodination-based studies, ultimately driving advancements in their respective fields.
This versatile technique is widely employed in scientific research and medical applications.
Radiolabeling with radioactive iodine isotopes, such as 125I, is a common practice used for imaging, diagnostics, and modifying the properties of compounds.
Iodination plays a pivotal role in various fields, including biochemistry, pharmacology, and materials science.
To streamline iodination protocols and enhance reproducibility, researchers can leverage PubCompare.ai's AI-driven platform.
This cutting-edge technology helps identify the best procedures and products from literature, preprints, and patents.
By utilizing AI-driven comparisons, researchers can optimize their iodination workflows and improve experimental outcomes.
The iodination process can be facilitated using a range of specialized products, such as Pierce Pre-Coated Iodination Tubes, Na125I, Pierce Iodination Beads, and Pierce Iodination Reagent.
Pre-coated iodination tubes and [125I]NaI provide convenient options for radiolabeling, while Pierce™ Iodination Tubes and Quick Spin Protein Columns can be used to purify and isolate iodinated compounds.
The availability of 125I stock solution and PD-10 columns further enhances the versatility of iodination research.
PubCompare.ai's AI-driven platform is a valuable resource for researchers looking to optimize their iodination protocols and streamline their experimental processes.
By leveraging this cutting-edge technology, scientists can enhance the reproducibility and efficacy of their iodination-based studies, ultimately driving advancements in their respective fields.