Eissa, Ibrahim H. team published research on Bioorganic Chemistry in 2021 | 144-48-9

HPLC of Formula: 144-48-9, 2-Iodoacetamide is a synthetic retinoid that binds to the DNA of cells, altering transcription. It also has been found to be effective in treating bowel disease and has been shown to have dna binding activity. The compound was synthesized by attaching iodine molecules to acetamide. 2-Iodoacetamide targets the protein thiols on the surface of cells, which are responsible for oxidation and damage due to reactive oxygen species (ROS). This compound is metabolized by alcohol dehydrogenase and can be used as a biological sample or natural compound is a compound used as an electrophile for covalent modification of nucleophilic residues on proteins (cysteine, methionine, histidine). When modifying the active-site residues of cysteine proteases, α-Iodoacetamide acts as an irreversible inhibitor of these enzymes.

2-Iodoacetamide used in peptide mapping because it covalently binds with thiols in cysteine residues, thereby preventing disulfide bond formation. By virtue of reaction with cysteine, it is an irreversible inhibitor of enzymes with cysteine at the active site. Also reacts with histidine residues though much more slowly, and this activity is responsible for inhibition of ribonuclease.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate., 144-48-9.

Iodide is one of the largest monatomic anions. It is assigned a radius of around 206 picometers. 144-48-9, formula is C2H4INO, Name is 2-Iodoacetamide.For comparison, the lighter halides are considerably smaller: bromide (196 pm), chloride (181 pm), and fluoride (133 pm). In part because of its size, iodide forms relatively weak bonds with most elements. HPLC of Formula: 144-48-9.

Eissa, Ibrahim H.;Dahab, Mohammed A.;Ibrahim, Mohamed K.;Alsaif, Nawaf A.;Alanazi, A. Z.;Eissa, Sally I.;Mehany, Ahmed B. M.;Beauchemin, Andre M. research published 《 Design and discovery of new antiproliferative 1,2,4-triazin-3(2H)-ones as tubulin polymerization inhibitors targeting colchicine binding site》, the research content is summarized as follows. Thirty-five new colchicine binding site inhibitors was designed and synthesized based on the 1,2,4-triazin-3(2H)-one nucleus I [n= 1, 2; R = NH2, OH, OEt; R1= R2= R3 = R4= H; R1= R2= R3 = R4 = OMe; R1= OMe, R2, R3, R4 = H, etc.]. Such mols. I were synthesized through a cascade reaction between readily accessible α-amino ketones and Ph carbazate as a masked N-isocyanate precursor. The synthesized derivatives I were cisoid restricted combretastatin A4 analogs containing 1,2,4-triazin-3(2H)-one in place of the olefinic bond, and they had the same essential pharmacophoric features of colchicine binding site inhibitors. The synthesized compounds I were evaluated in-vitro for their antiproliferative activities against a panel of three human cancer cell lines (MCF-7, HepG-2, and HCT-116), using colchicine as a pos. control. Among them, two compounds I [n= 2; R = OH; R1, R2 ,R4 = OMe, R3 = H] and I [n= 2; R = NH2; R1, R2 ,R4 = OMe, R3 = H] demonstrated a significant antiproliferative effect against all cell lines with IC50 ranging from 8.2 – 18.2μM. Further investigation was carried out for the most active cytotoxic agents as tubulin polymerization inhibitors. Compounds I [n= 2; R = OH; R1, R2 ,R4 = OMe, R3 = H] and I [n= 2; R = NH2; R1, R2 ,R4 = OMe, R3 = H] effectively inhibited microtubule assembly with IC50 values ranging from 3.9 to 7.8μM. Tubulin polymerization assay results were found to be comparable with the cytotoxicity results. The cell cycle anal. revealed significant G2/M cell cycle arrest of the analog I [n= 2; R = OH; R1, R2 ,R4 = OMe, R3 = H] in HepG-2 cells. The most active compounds I [n= 2; R = OEt; R1, R2 ,R4 = OMe, R3 = H], I [n= 2; R = OEt; R1, R2 ,R3 = R4 = OMe], I [n= 2; R = OH; R1= OMe, R2, R3, R4 = H], I [n= 2; R = OH; R1, R2, R4 = OMe, R3 = H] and I [n= 2; R = NH2; R1, R2 ,R4 = OMe, R3 = H] did not induce significant cell death in normal human lung cells Wl-38, suggesting their selectivity against cancer cells. Also, these compounds upregulated the level of active caspase-3 and boosted the levels of the pro-apoptotic protein Bax by five to seven folds in comparison to the control. Moreover, apoptosis analyses were conducted for compound I [n= 2; R = OH; R1, R2 ,R4 = OMe, R3 = H] evaluated its apoptotic potential. Finally, in-silico studies were conducted and revealed the probable interaction with the colchicine binding site. ADME prediction of the designed compounds I showed that they were not only with promising tubulin polymerization inhibitory activity but also with favorable pharmacokinetic and drug-likeness properties.

HPLC of Formula: 144-48-9, 2-Iodoacetamide is a synthetic retinoid that binds to the DNA of cells, altering transcription. It also has been found to be effective in treating bowel disease and has been shown to have dna binding activity. The compound was synthesized by attaching iodine molecules to acetamide. 2-Iodoacetamide targets the protein thiols on the surface of cells, which are responsible for oxidation and damage due to reactive oxygen species (ROS). This compound is metabolized by alcohol dehydrogenase and can be used as a biological sample or natural compound is a compound used as an electrophile for covalent modification of nucleophilic residues on proteins (cysteine, methionine, histidine). When modifying the active-site residues of cysteine proteases, α-Iodoacetamide acts as an irreversible inhibitor of these enzymes.

2-Iodoacetamide used in peptide mapping because it covalently binds with thiols in cysteine residues, thereby preventing disulfide bond formation. By virtue of reaction with cysteine, it is an irreversible inhibitor of enzymes with cysteine at the active site. Also reacts with histidine residues though much more slowly, and this activity is responsible for inhibition of ribonuclease.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate., 144-48-9.

Referemce:
Iodide – Wikipedia,
Iodide – an overview | ScienceDirect Topics – ScienceDirect.com