375853-73-9

Upstream product

• 375853-65-9 4-{3-[N,N-bis-(tert-butoxycarbonyl)aminomethyl]-phenyl}-piperidine 
• 10601-99-7 3-ethynylbenzoic acid 
• 286961-15-7 benzyl 4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)-3,6-dihydro-1 (2H)-pyridinecarboxylate 
• 286961-24-8 benzyl 1,2,3,6-tetrahydro-4-(trifluoromethylsulphonyloxy)-pyridine-1-carboxylate 
• 823-78-9 meta-bromobenzyl bromide 
• 51779-32-9 iminodicarboxylic acid di-tert-butyl ester 
• 19099-93-5 benzyl 4-oxo-1-piperidinecarboxylate 
• 851961-34-7 C₃₀H₃₈N₂O₆ 
• 375853-63-7 B-{3-[N,N-bis-(tert-butoxycarbonyl)aminomethyl]-phenyl}-pinacolato-boron 

Downstream Products

• 375853-75-1 N,N-bis-(tert-butoxycarbonyl)-3-[1-(3-phenylethynyl-benzoyl)-piperidin-4-yl]-benzylamine 
• 1374037-23-6 C₃₇H₄₁FN₂O₅ 
• 1374037-22-5 C₆₂H₇₄N₄O₁₀ 
• 1374037-20-3 C₄₂H₅₀N₄O₂ 
• 1374037-19-0 C₄₂H₄₂N₄O₂ 

Relevant academic research and scientific papers

Dimerization of β-tryptase inhibitors, does it work for both basic and neutral P1 groups?

The tetrameric folding of β-tryptase and the pair-wise distribution of its substrate binding sites offer a unique opportunity for development of inhibitors that span two adjacent binding sites. A series of dimeric inhibitors with two basic P1 moieties was

Structure based design of 4-(3-aminomethylphenyl)piperidinyl-1-amides: Novel, potent, selective, and orally bioavailable inhibitors of βII tryptase

Tryptase is a serine protease found almost exclusively in mast cells. It has trypsin-like specificity, favoring cleavage of substrates with an arginine (or lysine) at the P1 position, and has optimal catalytic activity at neutral pH. Current evidence suggests tryptase β is the most important form released during mast cell activation in allergic diseases. It is shown to have numerous pro-inflammatory cellular activities in vitro, and in animal models tryptase provokes broncho-constriction and induces a cellular inflammatory infiltrate characteristic of human asthma. Screening of in-house inhibitors of factor Xa (a closely related serine protease) identified β-amidoester benzamidines as potent inhibitors of recombinant human βII tryptase. X-ray structure driven template modification and exchange of the benzamidine to optimize potency and pharmacokinetic properties gave selective, potent and orally bioavailable 4-(3-aminomethyl phenyl)piperidinyl-1-amides.