74214-38-3

Usage

Uses

H-Leu-Phe-NH2 HCl

Upstream product

• 33900-15-1 (2S)-N-[(1S)-2-amino-1-benzyl-2-oxoethyl]-2-[(tert-butoxycarbonyl)amino]-4-methylpentanamide 
• 5241-58-7 L-Phenylalanine amide 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 

Downstream Products

• 109064-95-1 <4(S)--2,2-difluoro-3(R)-hydroxy-6-methylheptanoyl>-L-leucyl-L-phenylalaninamide 
• 109121-33-7 <4(S)--2,2-difluoro-3(R)-hydroxy-6-methyheptanoyl>-L-leucyl-L-phenylalaninamide 
• 93962-08-4 Boc-His-Sta-Leu-Phe-NH₂ 
• 794525-89-6 (5-(4-benzoyl-phenyl)-1S-benzyl-2R-(tert-butyldimethylsilanyloxy)-4R-(1-(1S-carbamoyl-2-phenyl-ethylcarbamoyl)-3(1S)-methyl-butylcarbamoyl)-pentyl)carbamic acid tert-butyl ester 
• 794525-88-5 {1S-benzyl-2R-(tert-butyldimethylsilanyloxy)-4R-[1-(1S-carbamoyl-2-phenyl-ethylcarbamoyl)-3-(1S)-methyl-butylcarbamoyl]-5-[4-(2-phenyl-[1.3]dioxolan-2-yl)phenyl]-pentyl}carbamic acid tert-butyl ester 
• 109064-97-3 <4(S)-amino-2,2-difluoro-3(R)-hydroxy-6-methylheptanoyl>-L-leucyl-L-phenylalaninamide trifluoroacetate 
• 87063-27-2 Boc-Phe-His-Sta-Leu-Phe-NH₂ 
• 98168-94-6 His-Sta-Leu-Phe-NH₂*2HCl 
• 87063-45-4 Ac-Phe-His-Sta-Leu-Phe-NH₂ 
• 93962-09-5 (phenoxyacetyl)-His-Sta-Leu-Phe-NH₂ 
• 452309-22-7 Nα-[3',5'-O-(tetraisopropyldisiloxane-1,3-diyl)uridin-2'-O-ylcarbonyl]-L-leucyl-L-phenylalaninamide 

Relevant academic research and scientific papers

Fluoro ketone containing peptides as inhibitors of human renin.

The pentapeptide BOC-Phe-Phe-difluorostatone-Leu-Phe-NH2 has been prepared and found to be a potent inhibitor of human renin. This compound contains a difluoromethylene ketone group that exists predominantly in the hydrated form in water. The difluorostat

Renin Inhibitors. Syntheses of Subnanomolar, Competitive, Transition-State Analogue Inhibitors Containing a Novel Analogue of Statine

Analogues of the renin octapeptide substrate were synthesized in which replacement of the scissile dipeptide with (3S,4S)-4-amino-3-hydroxy-6-methylheptanoic acid (statine, Sta) transformed the substrate sequence into potent, transition-state analogue, competitive inhibitors of renin.Synthesis and incorporation of the cyclohexylalanyl analogue of Sta, (3s,4S)-4-amino-5-cyclohexyl-3-hydroxypentanoic acid (ACHPA), gave the most potent inhibitors of renin yet reported, including N-isovaleryl-L-histydyl-L-prolyl-L-phenylalanyl-L-histydyl-ACHPA-L-leucyl-L-phenylalanyl amide , with renin inhibitions of Ki=1.6 * 10-10 M (human kidney renin), IC50=1.7 * 10-10 M (human plasma renin), IC50=1.9 * 10-9 M (dog plasma renin), and IC50=2.1 * 10-8 M (rat plasma renin).This inhibitor 3, containing ACHPA, was 55-76 times more potent vs. human renin than the comparable Sta-containing inhibitor 1 and 17 times more potent vs. dog renin than 1.Inhibitor 3 lowered blood pressure in sodium-deficient dogs, with in vivo potency 19 times that shown by 1, in close agreement with the relative in vitro potencies.Structure-activity results are presented that show the minimal N-terminus for these inhibitors.An ACHPA-containing pentapeptide, N--L-phenylalanyl-L-histydyl-ACHPA-L-lecyl-L-phenylalanyl amide , retained subnanomolar inhibitory potency.Molecular modelling studies are described that suggested the design of ACHPA.