635754-98-2

Upstream product

• 100-39-0 benzyl bromide 
• 21568-87-6 2-aminocaprolactam 
• 76944-95-1 tert-butyl N-[(3S)-2-oxoazepan-3-yl]carbamate 

Downstream Products

• 1361322-55-5 (S)-N-((S)-1-cyclohexyl-2-oxo-2-((S)-1-phenethylazepan-3-ylamino)ethyl)-2-(methylamino)propanamide 
• 1361323-06-9 tert-butyl (S)-1-((S)-1-cyclohexyl-2-oxo-2-((S)-1-phenethylazepan-3-ylamino)ethylamino)-1-oxopropan-2-yl(methyl)carbamate 
• 1361322-54-4 (S)-N-((S)-2-((S)-1-benzylazepan-3-ylamino)-1-cyclohexyl-2-oxoethyl)-2-(methylamino)propanamide 
• 1361323-05-8 tert-butyl (S)-1-((S)-2-((S)-1-benzylazepan-3-ylamino)-1-cyclohexyl-2-oxoethylamino)-1-oxopropan-2-yl(methyl)carbamate 
• 1361378-83-7 (S)-2-amino-N-((S)-1-benzylazepan-3-yl)-2-cyclohexylacetamide dihydrochloride 
• 1361323-03-6 tert-butyl (S)-2-((S)-1-benzylazepan-3-ylamino)-1-cyclohexyl-2-oxoethylcarbamate 
• 625471-23-0 (S)-1-benzylazepan-3-amine 

Relevant academic research and scientific papers

SUBSTITUTED ADIPIC ACID AMIDES AND USES THEREOF

The present invention provides compounds of Formula (I), or a pharmaceutically acceptable salt thereof, wherein A is a five to eight membered monocyclic or a nine to twelve membered bicyclic heterocyclic ring, as further defined herein; Y is S, CH2, or CH; Z is CH or N; R7 and R9 are hydrogen or (C1-C6)alkyl; R2 is (C1 C6)alkoxy, OH, CN, (C1-C6)alkyl, halogen, or CF3; r and s are 0, 1, or 2; and R1 and R3 are as further defined herein. These compounds are agonists, partial agonists and/or modulators of the NPY4 receptor and may be used for the treatment and prophylaxis of obesity, food intake, and other diseases and conditions modulated by the NPY4 receptor.

Discovery of aminopiperidine-based Smac mimetics as IAP antagonists

A series of structurally unique Smac mimetics that act as antagonists of inhibitor of apoptosis proteins (IAPs) has been discovered. While most previously described Smac mimetics contain the proline ring (or a similar cyclic motif) found in Smac, a key feature of the compounds described herein is that this ring has been removed. Despite this, compounds in this series potently bind to cIAP1 and elicit the expected phenotype of cIAP1 inhibition in cancer cells. Marked selectivity for cIAP1 over XIAP is observed for these compounds, which is attributed to a slight difference in the binding groove between the two proteins and the resulting steric interactions with the inhibitors. XIAP binding can be improved by constraining the inhibitor so that these unfavorable steric interactions are minimized.