96556-40-0

Upstream product

• 14002-80-3 Methyl 2,2-dimethyl-3-hydroxypropionate 
• 100-39-0 benzyl bromide 

Downstream Products

• 1229607-48-0 5-(benzyloxy)-4,4-dimethyl-3-oxopentanenitrile 
• 1404379-88-9 C₁₆H₂₂O₃ 
• 1404379-89-0 C₁₆H₂₄O₃ 
• 1404379-90-3 C₁₄H₂₀O₃ 
• 1404379-91-4 C₂₄H₂₉NO₄ 
• 1404379-92-5 C₃₀H₃₉NO₆ 
• 1404379-93-6 C₂₃H₃₃NO₆ 
• 1404379-96-9 C₃₉H₅₆O₄Si 
• 1404379-97-0 C₄₀H₅₉NO₄Si 
• 1404379-98-1 C₃₉H₅₆INO₄Si 
• 1404379-99-2 C₄₂H₆₁NO₄Si 
• 1404380-04-6 C₃₁H₄₄N₂O₄ 
• 1404377-87-2 C₃₀H₄₂N₂O₄ 
• 66582-32-9 3-(benzyloxy)-2,2-dimethylpropan-1-ol 

Relevant academic research and scientific papers

Synthesis and evaluation of prodrugs of corticotropin-releasing factor-1 (CRF1) receptor antagonist BMS-665053 leading to improved oral bioavailability

A series of phosphate and ester-based prodrugs of anilinopyrazinone 1 (BMS-665053) containing either a methylene or an (acyloxy)alkoxy linker was prepared and evaluated in rat pharmacokinetic studies with the goal of improving the oral bioavailability of the parent (1). The prodrugs, in general, had improved aqueous solubility and oral bioavailability compared to 1. Prodrug 12, which contains an (acyloxy)alkoxy linker, showed the greatest improvement in the oral bioavailability relative to the parent (1), with a seven-fold increase (from 5% to 36%) in rat pharmacokinetic studies.

AMIDE COMPOUND AND MEDICINAL USE THEREOF

A compound of formula [I-W]: wherein each symbol is as defined in the description, or a pharmaceutically acceptable salt thereof.

CGRP RECEPTOR ANTAGONISTS WITH TERTIARY AMIDE, SULFONAMIDE, CARBAMATE AND UREA END GROUPS

Compounds of formula I: (I) (wherein variables A, m, n, J, Re, Rf, R4, Ea, Eb, Ec, RPG and Y are as described herein) which are antagonists of CGRP receptors and which are useful

Mycothiazole: Synthesis of the C8-C18 subunit and further evidence of the (Z)-Δ14 double bond configuration

The synthesis of mycothiazole derivatives was undertaken in order to have further evidence of the C14-C15 double bond configuration. The recently revised (Z) configuration in the natural compound is consistent with the data found for our synthetic analogs

3-‘4-HETEROCYCLYL -1,2,3,-TRIAZOL-1-YL!-N-ARYL-BENZAMIDES AS INHIBITORS OF THE CYTOKINES PRODUCTION FOR THE TREATMENT OF CHRONIC INFLAMMATORY DISEASES

Disclosed compounds of formula (I), which inhibit production of cytokines involved in inflammatory processes and are thus useful for treating diseases and pathological conditions involving inflammation such as chronic inflammatory disease. Also disclosed are processes for preparing these compounds and pharmaceutical compositions comprising these compounds.

An unexpected formation of a 14-membered cyclodepsipeptide

The treatment of diluted solutions of the hydroxy diamides 6a and 6b in toluene with HCl gas at 100° gave the dimeric, 14-membered cyclodepsipeptide 10 in up to 72% yield (Scheme 3). The same product was formed from the linear dimer of 6b, the depsipeptid

O2-binding properties of double-sided porphinatoiron(II)s with polar substituents and their human serum albumin hybrids

Double-sided porphinatoiron(II)s with polar substituents [R; hydroxy (FeDP(OH)), methoxy (FeDP(OMe)), and acetoxy (FeDP(OAc))] on the 2,2-dimethylpropanoyloxy-fence groups have been synthesized. FeDP(OMe) and FeDP(OAc) formed five-N-coordinated high-spin Fe2+ complexes with an intramolecularly bound axial imidazole in toluene (or CH2Cl2) under an N2 atmosphere. Upon the addition of O2, they produced stable O2 adducts at 25 °C; their half-lives in water-saturated toluene (50-77 h) are 2-3 fold longer compared to that of the single-face encumbered porphinatoiron(II) (FeP). Their O2-binding parameters are almost identical to that of FeDP(H), which has nonpolar substituents on the fences. In contrast, FeDP(OH) showed a significantly low O2-binding affinity and was immediately oxidized to the Fe3+ state after contact with bubbling O2 gas. The incorporation of these FeDPs into the human serum albumin (HSA) provided artificial hemoproteins, which can reversibly bind and release O2 under physiological conditions (in aqueous media, pH 7.3, 37 °C) like hemoglobin and myoglobin. The half-life of the dioxygenated HSA-FeDP(H) reached 5 h (37 °C). This corresponded to a 2.5-fold increase compared to that of HSA-FeP. The time dependences of the absorption changes accompanying the O2- and CO-rebindings to the HSA-FeDPs after laser flash photolysis were composed of two phases. These observations indicate that the recombination of O2 and CO to the central Fe2+ ion is affected by the microenvironments around the FeDPs in the HSA structure, e.g. a steric hindrance of the amino acid residue and a difference in polarity. Furthermore, FeDP(H) incorporated into HSA showed a high stability against H2O2.