777939-69-2

Upstream product

• 501-53-1 benzyl chloroformate 
• 142034-78-4 (4aS,8aS)-Octahydro-2H-1,4-benzoxazin-3-one 
• 777939-68-1 (4aS,8aS,1'S)-N-(1'-phenyl)-ethyl-4-oxa-perhydrochinolin-2-on 
• 777939-67-0 (1S,2S,1'S)-N-2''-chloroacetyl-2-(1'-phenyl)-ethyl-aminocyclohexanol 
• 666845-36-9 trans-(1'S)2-N-[(α-phenylethyl)amino]cyclohexanol 
• 286-20-4 cyclohexene oxide 
• 931-15-7 (1S,2S)-trans-2-aminocyclohexanol 

Downstream Products

• 777939-72-7 [(1S,2S)-2-(2-{(1S,2S)-2-[(R)-2-((1S,2S)-2-Benzyloxycarbonylamino-cyclohexyloxy)-3-phenyl-propionylamino]-cyclohexyloxy}-acetylamino)-cyclohexyloxy]-acetic acid tert-butyl ester 
• 777939-71-6 (2R,1'S,2'S)-2-(2'-carboxybenzylamino-cyclohexyl)oxy-3-phenyl-propionic acid 
• 777939-70-5 (3R,4aS,8aS)-N-carboxybenzyl-3-benzyl-4-oxa-perhydrochinolin-2-on 

Relevant academic research and scientific papers

Folding propensity of cyclohexylether-δ-peptides

(Chemical Equation Presented) Linear (n = 2-18) and cyclic oligomers (n = 3-8) of a cyclohexylether-δ-amino acid (COA) were prepared in high yield and stereopurity. CD spectra of the linear oligomers were indicative of secondary structure formation. X-ray crystal structures of cyclic COA oligomers revealed hydrophobic packing and internal 5- and 10-membered-ring hydrogen bonds. Ether and amide oxygens reside preferably in an ap orientation. This conformational locking is apparently broken by a C-2 substituent in an asymmetric cyclotrimer, for which a zeolithe-like tubular structure was found.