18959-40-5

Upstream product

• 331-39-5 caffeic acid 
• 79-22-1 methyl chloroformate 

Downstream Products

• 16180-95-3 3,4-O-dimethoxycarbonyl caffeic acid chloride 
• 86632-03-3 3,4,5-tri-O-caffeoyl-quinic acid 
• 222320-23-2 bis(diphenylmethyl) bis-L-tartrate 
• 222320-56-1 bis(diphenylmethyl) bis-meso-tartrate 
• 222320-55-0 bis(diphenylmethyl) bis-D-tartrate 
• 222320-25-4 bis(diphenylmethyl) dicaffeoyl-L-tartrate 
• 222320-58-3 bis(diphenylmethyl) dicaffeoyl-meso-tartrate 
• 222320-57-2 bis(diphenylmethyl) dicaffeoyl-D-tartrate 
• 222320-61-8 1,4-cis-biscyclohexanediol 
• 222320-60-7 1,4-trans-biscyclohexanediol 

Relevant academic research and scientific papers

Interaction of chlorogenic acids and quinides from coffee with human serum albumin

Chlorogenic acids and their derivatives are abundant in coffee and their composition changes between coffee species. Human serum albumin (HSA) interacts with this family of compounds with high affinity. We have studied by fluorescence spectroscopy the spe

METHOD FOR MANUFACTURING 3,4,5-TRICAFFEOYLQUINIC ACID

Provided are a method for manufacturing 3,4,5-tricaffeoylquinic acid, which can produce 3,4,5-tricaffeoylquinic acid with high efficiency by a simple operation in a short process using inexpensive raw materials, and intermediate compounds. The method for manufacturing 3,4,5-tricaffeoylquinic acid of the invention includes at least Step (1) of allowing a compound represented by Formula (1) or a compound represented by Formula (2) to react with a compound represented by Formula (4); and Step (2) of deprotecting the product obtained in Step (1), and producing 3,4,5-tricaffeoylquinic acid:

Interaction of chlorogenic acids and quinides from coffee with human serum albumin

Chlorogenic acids and their derivatives are abundant in coffee and their composition changes between coffee species. Human serum albumin (HSA) interacts with this family of compounds with high affinity. We have studied by fluorescence spectroscopy the spe

Novel HIV integrase inhibitors and HIV therapy based on drug combinations including integrase inhibitors

The present invention includes a group of novel compounds that are demonstrated to potently and selectively inhibit HIV integrase (IN) activity in vitro and to potently inhibit HIV replication in live, cultured cells at non-toxic concentrations. The novel

Structure-activity relationships: Analogues of the dicaffeoylquinic and dicaffeoyltartaric acids as potent inhibitors of human immunodeficiency virus type 1 integrase and replication

The dicaffeoylquinic acids (DCQAs) and dicaffeoyltartaric acids (DCTAs) are potent and selective inhibitors of human immunodeficiency virus type 1 (HIV-1) integrase. They also inhibit HIV-1 replication at nontoxic concentrations. Since integrase is an excellent target for anti-HIV therapy, structure-activity relationships were employed to synthesize compounds with: (1) improved potency against HIV-1 integrase, (2) improved anti-HIV effect in tissue culture, and (3) increased selectivity as indicated by low cellular toxicity. Thirty-four analogues of the DCTAs and DCQAs were synthesized and tested for cell toxicity, anti-HIV activity, and inhibition of HIV-1 integrase. Seventeen of the 34 analogues had potent activity against HIV-1 integrase ranging from 0.07 to > 10 μM. Seventeen analogues that were synthesized or purchased had no inhibitory activity against integrase at concentrations of 25 μM. Of the biologically active analogues, 7 of the 17 inhibited HIV replication at nontoxic concentrations. The most potent compounds were D-chicoric acid, meso-chicoric acid, bis(3,4- dihydroxydihydrocinnamoyl)-L-tartaric acid, digalloyl-L-tartaric acid, bis(3,4-dihydroxybenzoyl)-L-tartaric acid, dicaffeoylglyceric acid, and bis(3,4-dihydroxyphenylacetyl)-L-tartaric acid. Anti-HIV activity of the active compounds in tissue culture ranged from 35 to 0.66 μM. Structure- activity relationships demonstrated that biscatechol moieties were absolutely required for inhibition of integrase, while at least one free carboxyl group was required for anti-HIV activity. These data demonstrate that analogues of the DCTAs and the DCQAs can be synthesized which have improved activity against HIV integrase.