3057-26-9

Upstream product

• 5331-43-1 N-benzyloxycarbonyl-hydrazine 
• 67-64-1 acetone 
• 77-76-9 2,2-dimethoxy-propane 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 29134-54-1 tris(benzyloxy)methane 
• 3057-25-8 benzyl 2-isopropylhydrazine-1-carboxylate 
• 1451983-13-3 2-benzyl 1-tert-butyl 1-isopropylhydrazine-1,2-dicarboxylate 
• 3459-92-5 DBC 
• 300594-28-9 2,2-dibenzyloxy-5,5-dimethyl-Δ³-1,3,4-oxadiazoline 

Relevant academic research and scientific papers

Rational Drug Design of Topically Administered Caspase 1 Inhibitors for the Treatment of Inflammatory Acne

The use of an interleukin β antibody is currently being investigated in the clinic for the treatment of acne, a dermatological disorder affecting 650M persons globally. Inhibiting the protease responsible for the cleavage of inactive pro-IL1β into active IL-1β, caspase-1, could be an alternative small molecule approach. This report describes the discovery of uracil 20, a potent (38 nM in THP1 cells assay) caspase-1 inhibitor for the topical treatment of inflammatory acne. The uracil series was designed according to a published caspase-1 pharmacophore model involving a reactive warhead in P1 for covalent reversible inhibition and an aryl moiety in P4 for selectivity against the apoptotic caspases. Reversibility was assessed in an enzymatic dilution assay or by using different substrate concentrations. In addition to classical structure-activity-relationship exploration, topical administration challenges such as phototoxicity, organic and aqueous solubility, chemical stability in solution, and skin metabolic stability are discussed and successfully resolved.

New Schiff bases derived from benzyl carbazate with alkyl and heteroaryl ketones: Isolation, structural characterization, thermal behavior and molecular docking studies

The condensation reaction of benzyl carbazate with the ketones, viz., dimethylketone, dipropylketone, cyclobutanone, cyclopentanone, cyclohexanone, cycloheptanone, 2-acetylpyridine, 3-acetylpyridine and 4-acetylpyridine, yielded the Schiff bases [benzyl 2

E-64c-hydrazide: A lead structure for the development of irreversible cathepsinc inhibitors

CathepsinC is a papain-like cysteine protease with dipeptidyl aminopeptidase activity that is thought to activate various granule-associated serine proteases. Its exopeptidase activity is structurally explained by the so-called exclusion domain, which blocks the active-site cleft beyond the S2 site and, with its Asp1 residue, provides an anchoring point for the Nterminus of peptide and protein substrates. Here, the hydrazide of (2S,3S)-trans-epoxysuccinyl-L-leucylamido-3-methylbutane (E-64c) (k2/Ki=140±5M-1s-1) is demonstrated to be a lead structure for the development of irreversible cathepsinC inhibitors. The distal amino group of the hydrazide moiety addresses the acidic Asp1 residue at the entrance of the S2 pocket by hydrogen bonding while also occupying the flat hydrophobic S1′-S2′ area with its leucine-isoamylamide moiety. Furthermore, structure-activity relationship studies revealed that functionalization of this distal amino group with alkyl residues can be used to occupy the conserved hydrophobic S2 pocket. In particular, the n-butyl derivative was identified as the most potent inhibitor of the series (k2/Ki=56000±1700M-1s-1).

Benzyloxy(4-substituted benzyloxy)carbenes. Generation from oxadiazolines and fragmentation to radical pairs in solution

Thermolysis of 2,2-dibenzyloxy-5,5-dimethyl-Δ3-1,3,4-oxadiazoline in benzene at 110°C leads to dibenzyloxycarbene. The carbene was trapped with tert-butyl alcohol to afford dibenzyl-tert-butyl orthoformate. In the absence of a trapping agent for the carbene, it fragmented to benzyloxycarbonyl and benzyl radicals, as shown by trapping the latter with TEMPO. In the absence of both TEMPO and tert-butyl alcohol, the radicals were partitioned between coupling to benzyl phenylacetate and decarboxylation, with subsequent formation of bibenzyl. The preferred sense of fragmentation of the analogous carbenes from benzyloxy-(p-substituted-benzyloxy)carbenes was determined by comparing the yields of the two possible esters, ArCH2O(CO)CH2Ph and PhCH2O(CO)CH2Ar. It was found that an electron-withdrawing group in the para position favoured fragmentation to the benzylic radical containing that group. A Hammett plot of the data gave a best fit with σ- substituent constants (r = 0.994, ρ((PhH, 110°C) = 0.7)) suggesting that the fragmentation involves charge separation in the sense that increases electron density on the group that is becoming a benzylic radical and decreases electron density on the carbonyl group that is becoming the benzyloxycarbonyl radical.

Sodium cyanoborohydride reduction of (benzyloxycarbonyl)- and (tert-butoxycarbonyl)hydrazones

(Benzyloxycarbonyl)- and (tert-butoxycarbonyl)hydrazones are easily reduced by sodium cyanoborohydride in acidic medium. The method is an alternative to catalytic hydrogenation and allows ready access to both N-benzyloxycarbonyl and N-tert-butoxycarbonyl

ORGANISCHE PHOSPHORVERBINDUNGEN 84. HERSTELLUNG, EIGENSCHAFTEN UND BIOLOGISCHE WIRKUNG VON HYDRAZINOMETHYL-PHOSPHON- UND -PHOSPHINSAEUREN UND DERIVATEN

The synthesis and the chemical, physical, spectral and biological properties of hydrazinomethyl-phosphonic- and -phosphinic acids and derivatives, i.e. hydrazino-N-alkoxycarbonyl-N'-alkylene-O,O-dialkoxyphosphonates, 2, -phosphinates, 3, hydrazinomethyl-O