3054-07-7

Usage

Chemical Properties

White to off-white crystalline powder

InChI:InChI=1/C8H15NO4/c9-6(8(12)13)4-2-1-3-5-7(10)11/h6H,1-5,9H2,(H,10,11)(H,12,13)/p-1/t6-/m1/s1

Upstream product

• 24479-92-3 2-chloro-octanedioic acid 
• 496921-59-6 1,1-diethyl 6-methyl 1-acetamidohexane-1,1,6-tricarboxylate 
• 24479-85-4 8,8-dichloro-oct-7-enoic acid 
• 14273-91-7 methyl 6-iodohexanoate 
• 1068-90-2 2-acetylaminomalonic acid diethyl ester 
• 14273-90-6 methyl 6-bromohexanoate 
• 6415-47-0 2-bromo-octanedioic acid dimethyl ester 
• 25542-62-5 6-bromo-hexanoic acid ethyl ester 
• 119808-28-5 Diethyl 2-acetamido-2-ethoxycarbonyloctanedioate 
• 6628-78-0 6-chlorohexanenitrile 

Downstream Products

• 533-48-2 (+/-)-6-(5t-methyl-2-oxo-imidazolidin-4r-yl)-hexanoic acid 
• 533-48-2 dl-dethiobiotine 
• 496876-03-0 H2N-Phe-(R)Pro-Asu-βhPhe-OH 
• 1208999-99-8 2-(((9H-fluoren-9-yl)methoxy)carbonylamino)octanedioic acid 
• 292642-79-6 2-(tert-butoxycarbonylamino)octanedioic acid 
• 4254-88-0 (2S)-L-α-Aminosuberic acid 
• 19641-63-5 (2R)-D-α-Aminosuberic acid 
• 19641-67-9 N-Carbobenzoxy-D-α-aminosuberinsaeure 
• 119808-29-6 Z-Asu-OH 
• 19641-64-6 N-(benzyloxycarbonyl)-L-α-aminosuberic acid 
• 4793-80-0 6-(5-methyl-2-oxo-2,3-dihydro-1H-imidazol-4-yl)-hexanoic acid 

Relevant academic research and scientific papers

Inhibitors selective for HDAC6 in enzymes and cells

Histone deacetylase inhibitors with anticancer or anti-inflammatory activity bind to Class I or Class I and II HDAC enzymes. Here we compare selectivity of inhibitors of a Class II HDAC enzyme (HDAC6) and find one that retains high selectivity in macrophages.

Antimalarial histone deacetylase inhibitors containing cinnamate or NSAID components

Malaria is the most lethal parasite-mediated tropical infectious disease, killing 1-2 million people each year. An emerging drug target is the enzyme Plasmodium falciparum histone deacetylase 1 (PfHDAC1). We report 26 compounds designed to bind the zinc and exterior surface around the entrance to the active site of PfHDAC1, 16 displaying potent in vitro antimalarial activity (IC 50 10-fold more cytotoxic towards P. falciparum than a normal human cell type (NFF). Twenty-two inhibitors feature cinnamic acid derivatives or non-steroidal anti-inflammatory drugs (NSAIDs) as HDAC-binding components. A homology model of PfHDAC1 enzyme gives new insights to interactions likely made by some of these inhibitors. Results support PfHDAC1 as a promising new antimalarial drug target.

INHIBITORS OF KYNURENINE AMINOTRANSFERASE AND USES THEREFOR

Provided herein are methods of decreasing a level of kynurenic acid in a cell and of treating a pathophysiological condition in a subject associated with an increase in kynurenic acid in a subject. In these methods the inhibitory action of dicarboxylic acids or derivatives or analogs thereof are effective to inhibit activity of kynurenine aminotransferase II. Also provided is a method of screening for potential inhibitory compounds for kynurenine aminotransferase II. The dicarboxylic acids or derivatives or analogs thereof may have the structural formula, where R1 is H, NH2 or NHCH3, R2 is H or CH3, n is 0 to 14, and X is -COOH, CH2OH, -PO3H2, -SO2H, or -SO3H; or a pharmacologically acceptable salt.

Design, synthesis, potency, and cytoselectivity of anticancer agents derived by parallel synthesis from α-aminosuberic acid

Chemotherapy in the last century was characterized by cytotoxic drugs that did not discriminate between cancerous and normal cell types and were consequently accompanied by toxic side effects that were often dose limiting. The ability of differentiating agents to selectively kill cancer cells or transform them to a nonproliferating or normal phenotype could lead to cell- and tissue-specific drugs without the side effects of current cancer chemotherapeutics. This may be possible for a new generation of histone deacetylase inhibitors derived from amino acids. Structure-activity relationships are now reported for 43 compounds derived from 2-aminosuberic acid that kill a range of cancer cells, 26 being potent cytotoxins against MM96L melanoma cells (IC50 20 nM-1 μM), while 17 were between 5- and 60-fold more selective in killing MM96L melanoma cells versus normal (neonatal foreskin fibroblasts, NFF) cells. This represents a 10- to 100-fold increase in potency and up to a 10-fold higher selectivity over previously reported compounds derived from cysteine (J. Med. Chem. 2004, 47, 2984). Selectivity is also an underestimate, because the normal cells, NFF, are rarely all killed by the drugs that also induce selective blockade of the cell cycle for normal but not cancer cells. Selected compounds were tested against a panel of human cancer cell lines (melanomas, prostate, breast, ovarian, cervical, lung, and colon) and found to be both selective and potent cytotoxins (IC50 20 nM-1 μM). Compounds in this class typically inhibit human histone deacetylases, as evidenced by hyperacetylation of histones in both normal and cancer cells, induce expression of p21, and differentiate surviving cancer cells to a nonproliferating phenotype. These compounds may be valuable leads for the development of new chemotherapeutic agents.

Process for producing alpha 2,3/ alpha 2,8-sialyltransferase and sialic acid-containing complex sugar

The present invention can provide a process for producing a protein having α2,3/α2,8-sialyltransferase activity using a transformant comprising a DNA encoding a protein having α2,3/α2,8-sialyltransferase activity derived from a microorganism belonging to the genus Pasteurella and a process for producing a sialic acid-containing complex carbohydrate using a transformant capable of producing a protein having α2,3/α2,8-sialyltransferase activity derived from a microorganism.

Conformationally homogeneous cyclic tetrapeptides: Useful new three-dimensional scaffolds

The most commonly recognized motifs in protein-protein interactions are γ and β turns, which are defined by three to four contiguous amino acids in a peptide sequence. Cyclic tetrapeptides thus represent minimalist turn mimetics, but their usefulness is c

Human CDR-grafted antibody and antibody fragment thereof

A human CDR-grafted antibody or the antibody fragment thereof which specifically reacts with the extracellular region of human CC chemokine receptor 4 (CCR4) but does not react with a human blood platelet; a human CDR-grafted antibody or the antibody fragment thereof which specifically reacts with the extracellular region of CCR4 and has a cytotoxic activity against a CCR4-expressing cell; and a medicament, a therapeutic agent or a diagnostic agent comprising at least one of the antibodies and the antibody fragments thereof as an active ingredient.

Gene recombinant antibody and antibody fragment thereof

A recombinant antibody or the antibody fragment thereof which specifically reacts with an extracellular domain of human CCR4; a DNA which encodes the recombinant antibody or the antibody fragment thereof; a method for producing the recombinant antibody or the antibody fragment thereof; a method for immunologically detecting CCR4, a method for immunologically detecting a cell which expressed CCR4 on the cell surface, a method for depleting a cell which expresses CCR4 on the cell surface, and a method for inhibiting production of Th2 cytokine, which comprise using the recombinant antibody according or antibody fragment thereof; a therapeutic or diagnostic agent for Th2-mediated immune diseases; and a therapeutic or diagnostic agent for a blood cancer.

Tandem enzymatic resolution yielding L-α-aminoalkanedioic acid ω-esters

The tandem action of serine protease (α-chymotrypsin or subtilisin BPN') and Aspergillus genus aminoacylase on racemic N-acetyl-α-aminoalkanedioic acid α,ω-diester produced L-α-aminoalkanedioic acid ω-ester in good yield and high optical purity. L-α-Amino

Synthesis and platelet aggregation inhibiting activity of acid side-chain modified hydantoin prostaglandin analogues

A series of hydantoin prostaglandin analogues, in which the hexamethylene moiety of the acid side chain was replaced by other spacing groups possessing either ether, sulphide and/or olefin functionality, were prepared and evaluated for platelet aggregation inhibiting activity. The 4-thia analogue 13 proved to be the most potent inhibitor (ca. 22x PGE1) and the 3-thia- and 3-oxa-analogues, 6 and 10 respectively, are approximately equipotent with BW245C (ca. 14x PGE1). Z-olefinic analogues (e.g. 11) were usually more potent than their E-isomers (e.g. 12). Structure-activity relationships are discussed in detail.