32024-15-0

Usage

Uses

Used in Chemical Synthesis:
3-Iodo-4,5-dimethoxybenzaldehyde is used as a key intermediate in the synthesis of complex organic molecules. Its unique structure allows for further functionalization and incorporation into a wide range of compounds.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, 3-Iodo-4,5-dimethoxybenzaldehyde is used as a starting material for the synthesis of various bioactive compounds, such as chloropeptin I and chloropeptin II. These compounds have potential applications in the development of new drugs targeting specific medical conditions.
Used in Organic Chemistry Research:
3-Iodo-4,5-dimethoxybenzaldehyde serves as a valuable research tool in organic chemistry, enabling the exploration of new reaction pathways and the development of innovative synthetic methods. Its reactivity and structural features make it an attractive candidate for studying various chemical transformations and mechanisms.

InChI:InChI=1/C9H9IO3/c1-12-8-4-6(5-11)3-7(10)9(8)13-2/h3-5H,1-2H3

Upstream product

• 5438-36-8 5-iodovaniline 
• 77-78-1 dimethyl sulfate 
• 74-88-4 methyl iodide 
• 121-33-5 vanillin 
• 89942-36-9 2-iodo-4-hydroxy-3-methoxybenzaldehyde 
• 54246-05-8 3-iodo-4,5-dihydroxybenzaldehyde 
• 54246-07-0 3-hydroxy-5-iodo-4-methoxybenzaldehyde 

Downstream Products

• 4482-29-5 2,2’,3,3’-tetramethoxy-5,5’-diformyl-1,1’-biphenyl 
• 120-14-9 3,4-dimethoxy-benzaldehyde 
• 90888-39-4 1-Jod-2,3-dimethoxy-5-(1-hydroxy-2-nitro-aethyl)-benzol 
• 83166-73-8 5-(3-iodo-4,5-dimethoxy-benzyl)-pyrimidine-2,4-diamine 
• 67483-49-2 3,4-dimethoxy-5-(prop-2-enyl)benzaldehyde 
• 692779-51-4 4-[5-(2,4-diamino-pyrimidin-5-ylmethyl)-2,3-dimethoxy-phenylethynyl]-benzoic acid ethyl ester 
• 692779-46-7 6-[5-(2,4-diamino-pyrimidin-5-ylmethyl)-2,3-dimethoxy-phenyl]-hex-5-ynoic acid benzyl ester 
• 50772-81-1 methyl 3-iodo-4,5-dimethoxybenzoate 

Relevant academic research and scientific papers

Targeting telomerase with radiolabeled inhibitors

The expression of telomerase in approximately 85% of cancers and its absence in the majority of normal cells makes it an attractive target for cancer therapy. However the lag period between initiation of telomerase inhibition and growth arrest makes direct inhibition alone an insufficient method of treatment. However, telomerase inhibition has been shown to enhance cancer cell radiosensitivity. To investigate the strategy of simultaneously inhibiting telomerase while delivering targeted radionuclide therapy to cancer cells,123I-radiolabeled inhibitors of telomerase were synthesized and their effects on cancer cell survival studied. An123I-labeled analogue of the telomerase inhibitor MST-312 inhibited telomerase with an IC50of 1.58?μM (MST-312 IC50: 0.23?μM). Clonogenic assays showed a dose dependant effect of123I-MST-312 on cell survival in a telomerase positive cell line, MDA-MB-435.

Inhibitor design to target a unique feature in the folate pocket of Staphylococcus aureus dihydrofolate reductase

Staphylococcus aureus (Sa) is a serious concern due to increasing resistance to antibiotics. The bacterial dihydrofolate reductase enzyme is effectively inhibited by trimethoprim, a compound with antibacterial activity. Previously, we reported a trimethoprim derivative containing an acryloyl linker and a dihydophthalazine moiety demonstrating increased potency against S. aureus. We have expanded this series and assessed in vitro enzyme inhibition (Ki) and whole cell growth inhibition properties (MIC). Modifications were focused at a chiral carbon within the phthalazine heterocycle, as well as simultaneous modification at positions on the dihydrophthalazine. MIC values increased from 0.0626–0.5 μg/mL into the 0.5–1 μg/mL range when the edge positions were modified with either methyl or methoxy groups. Changes at the chiral carbon affected Ki measurements but with little impact on MIC values. Our structural data revealed accommodation of predominantly the S-enantiomer of the inhibitors within the folate-binding pocket. Longer modifications at the chiral carbon, such as p-methylbenzyl, protrude from the pocket into solvent and result in poorer Ki values, as do modifications with greater torsional freedom, such as 1-ethylpropyl. The most efficacious Ki was 0.7 ± 0.3 nM, obtained with a cyclopropyl derivative containing dimethoxy modifications at the dihydrophthalazine edge. The co-crystal structure revealed an alternative placement of the phthalazine moiety into a shallow surface at the edge of the site that can accommodate either enantiomer of the inhibitor. The current design, therefore, highlights how to engineer specific placement of the inhibitor within this alternative pocket, which in turn maximizes the enzyme inhibitory properties of racemic mixtures.

Halogenated trimethoprim derivatives as multidrug-resistant Staphylococcus aureus therapeutics

Incorporation of halogen atoms to drug molecule has been shown to improve its properties such as enhanced in membrane permeability and increased hydrophobic interactions to its target. To investigate the effect of halogen substitutions on the antibacterial activity of trimethoprim (TMP), we synthesized a series of halogen substituted TMP and tested for their antibacterial activities against global predominant methicillin resistant Staphylococcus aureus (MRSA) strains. Structure-activity relationship analysis suggested a trend in potency that correlated with the ability of the halogen atom to facilitate in hydrophobic interaction to saDHFR. The most potent derivative, iodinated trimethoprim (TMP-I), inhibited pathogenic bacterial growth with MIC as low as 1.25 μg/mL while the clinically used TMP derivative, diaveridine, showed resistance. Similar to TMP, synergistic studies indicated that TMP-I functioned synergistically with sulfamethoxazole. The simplicity in the synthesis from an inexpensive starting material, vanillin, highlighted the potential of TMP-I as antibacterial agent for MRSA infections.

Chemoselective zinc/HCl reduction of halogenated β-nitrostyrenes: Synthesis of halogenated dopamine analogues

A detailed account regarding the synthesis of 2- and 5-halogenated dopamine is given. The key step is a chemoselective reduction of a nitrostyrene by Zn/HCl at 0 °C. These conditions represent a simple, low-cost alternative to reduction by water-sensitive hydride donors and two-step procedures. Under these conditions, aryl fluoride, chloride, and bromide groups are stable. However, iodine undergoes significant reductive dehalogenation.

HIGHLY 6-SUBSTITUTED -2,4-DIAMINOPYRIMIDINES AS INHIBITORS OF ANTHRAX

2,4-diaminopyrimidine compounds of generic Formula 1, where R and R' may be the same or different and are independently selected from: C1-C6 alkyl or alkenyl groups with 1, 2, 3, 4, 5 or 6 carbon atoms, which may be: branched or unbranched; saturated or unsaturated; and may or may not be substituted, are used to treat anthrax.

Synthesis and biological activity of substituted 2,4-diaminopyrimidines that inhibit Bacillus anthracis

A series of substituted 2,4-diaminopyrimidines 1 has been prepared and evaluated for activity against Bacillus anthracis using previously reported (±)-3-{5-[(2,4-diamino-5-pyrimidinyl)methyl]-2,3-dimethoxyphenyl} -1-(1-propyl-2(1H)-phthalazinyl)-2-propen-1-one (1a), with a minimum inhibitory concentration (MIC) value of 1-3 μg/mL, as the standard. In the current work, the corresponding isobutenyl (1e) and phenyl (1h) derivatives displayed the most significant activity in terms of the lowest MICs with values of 0.5 μg/mL and 0.375-1.5 μg/mL, respectively. It is likely that the S isomers of 1 will bind the substrate-binding pocket of dihydrofolate reductase (DHFR) as in B. anthracis was found for (S)-1a. The final step in the convergent synthesis of target systems 1 from (±)-1-(1-substituted-2(1H)- phthalazinyl)-2-propen-1-ones 6 with 2,4-diamino-5-(5-iodo-3,4-dimethoxybenzyl) pyrimidine (13) was accomplished via a novel Heck coupling reaction under sealed-tube conditions.

Inhibition of Bacterial Dihydrofolate Reductase by 6-Alkyl-2,4-diaminopyrimidines

(±)-6-Alkyl-2,4-diaminopyrimidine-based inhibitors of bacterial dihydrofolate reductase (DHFR) have been prepared and evaluated for biological potency against Bacillus anthracis and Staphylococcus aureus. Biological studies revealed attenuated activity relative to earlier structures lacking substitution at C6 of the diaminopyrimidine moiety, though minimum inhibitory concentration (MIC) values are in the 0.125-8μgmL-1 range for both organisms. This effect was rationalized from three- dimensional X-ray structure studies that indicate the presence of a side pocket containing two water molecules adjacent to the main binding pocket. Because of the hydrophobic nature of the substitutions at C6, the main interactions are with protein residues Leu20 and Leu28. These interactions lead to a minor conformational change in the protein, which opens the pocket containing these water molecules such that it becomes continuous with the main binding pocket. These water molecules are reported to play a critical role in the catalytic reaction, highlighting a new area for inhibitor expansion within the limited architectural variation at the catalytic site of bacterial DHFR.

SUBSTITUTED ISOQUINOLINES AND THEIR USE AS TUBULIN POLYMERIZATION INHIBITORS

The present invention relates generally to substituted isoquinolines and their use as tubulin polymerization inhibitors. In particular, the invention relates to substituted isoquinolines which possess useful therapeutic activity, use of these compounds in methods of therapy and the manufacture of medicaments as well as compositions containing these compounds

Facile total synthesis of benzo[b]furan natural product XH-14

An efficient and practical total synthesis of benzo[b]furan natural product XH-14 is demonstrated in nine steps from vanillin. Introduction of iodide substituents in the reaction including optimization of the reaction sequences is essential for the successful synthesis of XH-14. Sonogashira coupling with iodobenzene, iodine-induced cyclization, Wittig reaction, and formylation are critical in the high-yield total synthesis of XH-14. Copyright Taylor & Francis Group, LLC.