138563-68-5

Upstream product

• 5292-43-3 bromoacetic acid tert-butyl ester 
• 554-84-7 meta-nitrophenol 
• 138563-69-6 tert-butyl 2-(3-nitrophenoxy)acetate 

Downstream Products

• 184944-89-6 [3-(3-{1-[(Isopropyl-phenyl-carbamoyl)-methyl]-2,4-dioxo-5-phenyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]diazepin-3-yl}-ureido)-phenoxy]-acetic acid tert-butyl ester 
• 205694-20-8 tert-butyl 2-(3-{N-[2-(N-tert-butoxycarbonylamino)acetyl]amino}phenoxy)acetate 
• 919085-55-5 C₂₀H₂₀ClN₅O₃ 

Relevant academic research and scientific papers

Design, synthesis and immunological evaluation of novel amphiphilic desmuramyl peptides

Muramyl dipeptide (MDP) – an essential bacterial cell wall component – is recognized by our immune system as pathogen-associated molecular pattern (PAMP) which results in immune responses with adverse toxic effects. In order to harness the beneficial prop

Amphiphilic desmuramyl peptides for the rational design of new vaccine adjuvants: Synthesis, in vitro modulation of inflammatory response and molecular docking studies

Nucleotide-binding oligomerization domain 2 (NOD2) is cytosolic surveillance receptor of the innate immune system capable of recognizing the bacterial and viral infections. Muramyl dipeptide (MDP) is the minimal immunoreactive unit of murein. NOD2 perceives MDP as pathogen-associated molecular pattern, thereby triggering an immune response with undesirable side-effects. Beneficial properties of MDP, such as pro-inflammatory characteristics for the rational design of new vaccine adjuvants, can be harnessed by strategically re-designing the molecule. In this work, a new class of amphiphilic desmuramylpeptides (DMPs) were synthesized by replacing the carbohydrate moiety (muramic acid) of the parent molecule with hydrophilic arenes. A lipophilic chain was also introduced at the C-terminus of dipeptide moiety (alanine-isoglutamine), while conserving its L-D configuration. These novel DMPs were found to set off the release of higher levels of tumour necrosis factor alpha (TNF-α) than Murabutide, which is a well-known NOD2 agonist. Molecular docking studies indicate that all these DMPs bind well to NOD2 receptor with similar dock scores (binding energy) through a number of hydrogen bonding and hydrophobic/π interactions with several crucial residues of the receptor. More studies are needed to further assess their immunomodulatory therapeutic potential, as well as the possible involvement of NOD2 activation.

PPAR AGONIST COMPOUNDS, PREPARATION AND USES

The present invention relates to novel PPAR agonist compounds as well as pharmaceutical compositions containing them. The compounds according to the invention are of quite particular therapeutic interest, notably for treating diabetes and/or dyslipidemias, as well as for preventing cardiovascular pathologies.

Synthesis and bovine β3-adrenergic agonistic activities of a novel series of aryloxypropanolamines

We synthesized a novel series of 21 aryloxypropanolamine compounds characterized by N-alkyl, aralkyl, and aryl substituents. The compounds showed potent β3-adrenergic agonistic activities in Chinese hamster ovary cells expressing the bovine β3-adrenoceptors with Kact and Ki values of 4.2 ± 3.0 nM and 459 ± 169 nM respectively, for the ligand with the best compromise between potency and affinity. Structure-activity relationships are discussed.

Syntheses of HIV-protease inhibitors having a peptide moiety which binds to GP120

Some HIV-protease inhibitor derivatives having an N- carbomethoxycarbonyl-prolyl-phenylalanine benzyl ester (CPF) moiety as a binding site to gp120 were designed and synthesized. Almost all the compounds bearing CPF on the phenoxyacetyl group showed protease-inhibitory activity. Compounds 25a and 25b, which have the CPF moiety at the ortho- and meta- positions of the phenoxyacetyl group, respectively, had anti-HIV activity, although the others showed only protease-inhibitory activity. These results suggest that 25b binds to gp120 and inhibits HIV protease.

Synthesis of dipeptide-type human immunodeficiency virus (HIV) protease inhibitors with a binding unit to GP120

Some dipeptide-type human immunodeficiency virus (HIV) protease inhibitors derived from KNI-102, with a N-carbomethoxycarbonylprolyl- phenylalanine benzyl ester (CPF) moiety as a binding site to gp120, were synthesized. Compounds 11a showed 7 - 100 times higher HIV protease- inhibitory activity (11a; IC50 = 0.90 μg/ml, 1.1 μM) than the standard compound 3 or 4 (3; IC50 = 3.7 μg/ml, 7.7 μM, 4; IC50 = 75 μg/ml, 155 μM). Generally, the compounds substituted at the o-position of the phenoxyacetyl group 7a, 11a, 16a and 21a showed several times higher inhibitory activity than 3.

Synthesis of phenoxyacetic acid derivatives as highly potent antagonists of gastrin/cholecystokinin-B receptors

A novel series of phenoxyacetic acid derivatives was synthesized based on considerations of the three-dimensional structural similarity of YM022 and RP72540. The gastrin/cholecystokinin (CCK)-B and CCK-A receptor antagonist activities of these compounds were evaluated by investigation of their affinities for human gastrin/CCK-B receptors and human CCK-A receptors, respectively. It was found that N-methyl-N-phenyl-2-[2-[N-(N-methyl-N- phenyl-carbamoylmethyl)-N-[2-[3-(3- methylphenyl)ureido]acetyl]amino]phenoxy]acetamide (20k, DZ-3514) exhibited high affinity for gastrin/CCK-B receptors and high selectivity over CCK-A receptors.

Discovery of 1,5-benzodiazepines with peripheral cholecystokinin (CCK-A) receptor agonist activity (II): Optimization of the C3 amino substituent

Analogs of the previously reported 1,5-benzodiazepine peripheral cholecystokinin (CCK-A) receptor agonist 1 were prepared which explore substitution and/or replacement of the C-3 phenyl urea moiety. Agonist efficacy on the isolated guinea pig gallbladder (GPGB) was retained with a variety of substituted ureas and amide analogs. Three compounds were identified which were orally active in the mouse gallbladder emptying assay (MGBE). The 2-indolamide (52) and N-(carboxymethyl)-2-indolamide (54) derivatives had improved affinity for the human CCK-A receptor but reduced agonist efficacy on the GPGB. Neither indolamide was orally active in a rat feeding assay. In contrast, the (3-carboxyphenyl)urea derivative (29, GW7854) had moderately increased affinity for the human CCK-B receptor but was a potent full agonist on the GPGB and was orally active in both the MGBE and rat feeding assays. GW7854 was a full agonist (EC50 = 60 nM) for calcium mobilization on CHO K1 cells expressing hCCK-A receptors and a potent antagonist of CCK-8 (pA2 = 9.1) on CHO K1 cells expressing hCCK-B receptors. GW7854 is a potent mixed CCK-A agonist/CCK-B antagonist which is orally active in two in vivo models of CCK-A-mediated agonist activity.

N-phenyl-N-acetamidoglycinamides, their preparation and medicaments containing them

Compounds of formula: STR1 in which R1 represents a hydrogen atom or an alkyl, alkoxycarbonyl or an unsubstituted or substituted phenyl radical, R2 represents a hydrogen atom or an unsubstituted or substituted alkyl radical, R3 represents an alkyl, phenylalkyl, indanyl, cycloalkylalkyl or an unsubstituted or substituted phenyl radical, or R2 and R3 form a heterocycle together with the nitrogen atom to which they are attached, and R4 represents an unsubstituted or substituted phenyl radical, a naphthyl, indolyl or quinolyl radical or a phenylamino radical in which the phenyl ring is unsubstituted or substituted, their preparation and medicaments containing them.