106032-76-2

Upstream product

• 63930-50-7 (S)-(+)-3-benzyloxy-2-methylpropyl bromide 
• 58521-45-2 tert-butoxycarbonyl-L-leucinal 
• 108-24-7 acetic anhydride 
• 89028-19-3 (2R,4S,5S)-1-(benzyloxy)-5-<(tert-butyloxycarbonyl)amino>-4-hydroxy-2,7-dimethyloctane 
• 89028-19-3 N-(tert-butoxycarbonyl)-(2R,4RS,5S)-5-amino-1-(benzyloxy)-2,7-dimethyloctan-4-ol 

Relevant academic research and scientific papers

Inhibition of aminopeptidases by peptides containing ketomethylene and hydroxyethylene amide bond replacements

Inhibitors of aminopeptidase enzymes have been prepared by the synthesis of peptide substrate analogues in which the scissile amide bond has been replaced with the hydrolytically stable ketomethylene (-COCH2-) and hydroxyethylene [-CH(OH)CHsub

Synthetic and Enzyme Inhibition Studies of Pepstatin Analogues Containing Hydroxyethylene and ketomethylene Dipeptide Isosteres

Synthetic details for the preparation of a series of hydroxyethylene and ketomethylene dipeptide isosteres with control of stereochemistry at C(2) are described.Incorporation of the isosteres into peptide sequences derived from pepstatin afforded potent inhibitors of the aspartic protease porcine pepsin.When or was substituted with statine ((3S,4S)-4-amino-3-hydroxy-6-methylheptanoic acid), inhibitors equipotent to the parent compound were obtained, whereas was a much less effective replacement for statine.A similar trend was evident in the corresponding ketones.The finding that structural features for good substrates do not closely parallel those for good inhibitors is discussed.