125697-93-0

Usage

Uses

LAVENDUSTIN C is used as a potent tyrosine kinase inhibitor for its ability to inhibit EGF receptor-associated tyrosine kinase, pp60c-src(+) kinase, and Ca2+ calmodulin-dependent kinase II, making it a valuable compound in the field of cancer research and treatment.
Used in Pharmaceutical Industry:
LAVENDUSTIN C is used as an anticancer agent for its potent tyrosine kinase inhibitory activity, which can potentially be applied in the development of targeted therapies against various types of cancer.
Used in Research Applications:
LAVENDUSTIN C is used as a research tool for studying the roles and mechanisms of tyrosine kinases in cellular processes, as well as for identifying potential therapeutic targets in cancer and other diseases related to kinase dysregulation.

InChI:InChI=1/C14H13NO5/c16-10-2-4-12(17)8(5-10)7-15-9-1-3-13(18)11(6-9)14(19)20/h1-6,15-18H,7H2,(H,19,20)

Upstream product

• 1194-98-5 2,5-Dihydroxybenzaldehyde 
• 89-57-6 5-Aminosalicylic Acid 

Downstream Products

• 188292-98-0 Acetic acid 4-acetoxy-2-{[(4-acetoxy-3-tetradecylcarbamoyl-phenyl)-tert-butoxycarbonyl-amino]-methyl}-phenyl ester 
• 188292-96-8 Acetic acid 4-acetoxy-2-{[(4-acetoxy-3-hexylcarbamoyl-phenyl)-tert-butoxycarbonyl-amino]-methyl}-phenyl ester 
• 188292-93-5 Acetic acid 4-acetoxy-2-{[(4-acetoxy-3-methylcarbamoyl-phenyl)-tert-butoxycarbonyl-amino]-methyl}-phenyl ester 
• 188292-91-3 2-Acetoxy-5-[tert-butoxycarbonyl-(2,5-diacetoxy-benzyl)-amino]-benzoic acid 
• 188293-04-1 (2,5-Dihydroxy-benzyl)-(4-hydroxy-3-tetradecylcarbamoyl-phenyl)-carbamic acid tert-butyl ester 
• 188293-01-8 (2,5-Dihydroxy-benzyl)-(3-hexylcarbamoyl-4-hydroxy-phenyl)-carbamic acid tert-butyl ester 
• 188293-00-7 (2,5-Dihydroxy-benzyl)-(4-hydroxy-3-methylcarbamoyl-phenyl)-carbamic acid tert-butyl ester 
• 188292-90-2 5-[tert-Butoxycarbonyl-(2,5-dihydroxy-benzyl)-amino]-2-hydroxy-benzoic acid 

Relevant academic research and scientific papers

A versatile solid phase synthesis of lavendustin A and certain biologically active analogs

Reaction of aminomethylated polystyrene resin (8) with succinic anhydride, followed by esterification of the free carboxylic acid of the product 9 with 2,5-dihydroxybenzaldehyde (4), afforded the resin-linked aldehyde intermediate 10. The key intermediate 10 was converted into the protein-tyrosine kinase inhibitor lavendustin A and certain analogs through reductive amination and reductive alkylation steps, followed by cleavage from the resin. This method enables the preparation of a wide variety of lavendustin A analogs using combinatorial chemistry and parallel synthesis techniques.

Structure-activity relationships in a series of 5-[(2,5- dihydroxybenzyl)amino]salicylate inhibitors of EGF-receptor-associated tyrosine kinase: Importance of additional hydrophobic aromatic interactions

Potent inhibitors of EGF-dependent protein tyrosine kinase (PTK) activity were synthesized in a series of 5-[(2,5-dihydroxybenzyl)amino]salicylates. Several of these compounds inhibited EGF-dependent DNA synthesis in ER 22 cells with IC50 1 μ

Novel antiproliferative agents derived from lavendustin A

The active partial structure of the potent tyrosine kinase inhibitor lavendustin A was derivatized in the search for novel agents against cellular proliferation. The antiproliferative potential of the new derivatives was determined using the human keratin

Synthesis and Structure-Activity Studies of a Series of salicylates as Inhibitors of EGF Receptor-Associated Tyrosine Kinase Activity

The synthesis and structure-activity relationships of a series of salicylates and a series of salicylates as inhibitors of EGF receptor-associated tyrosine kinase activity are described.Their inhibitory potency was evaluated in vitro using ER 22 cell membranes (CCL 39 cells transfected with EGF receptor) as an enzyme source and the tridecapeptide RRSrc (RRLIEDAEYAARG) as substrate.Their cellular activity was measured by inhibition of the EGF-stimulated DNA synthesis of ER 22 cells.Chemical modifications were made to analyze the role of the different substituents.The amino series was found to be more active than the imino series.The hydroquinone moiety appears to be essential for tyrosine kinase inhibitory activity in the series of 5-salicylates.Comparison of the imino and amino series by molecular modeling techniques provides further evidence in support of the hypothesis that the important reduced linking chain, CH2NH allows the correct positioning of the 2,5-dihydroxybenzyl ring, possibly in a cis-like conformational arrangement.