6464-78-4

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 121-44-8 triethylamine 
• 543-27-1 isobutyl chloroformate 
• 6464-79-5 Z-Phe-Arg(NO₂)-OCH₃ 
• 2149-70-4 N^ω-nitro-L-arginine 
• 769922-77-2 (S)-benzyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 51298-62-5 _N^ω-nitro-L-arginine methyl ester hydrochloride 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 
• 2149-70-4 N-nitro-L-arginine 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 

Downstream Products

• 122701-21-7 N^α-benzyloxycarbonyl-L-histidyl=>L-phenylalanyl=>N^ω-nitro-L-arginine 
• 448963-33-5 C₃₀H₃₅N₇O₇ 
• 448963-40-4 C₃₇H₃₈N₈O₁₁ 
• 23827-59-0 N^α-L-phenylalanyl-L-arginine ; acetate 
• 50573-05-2 N^ω-nitro-N^α-L-phenylalanyl-L-arginine 

Relevant academic research and scientific papers

Efficient synthesis of peptides by extension at the N- and C-terminii of arginine

(Chemical Equation Presented) L-Nω-Nitroarginine and L-arginine were coupled with N-(Cbz-α-aminoacyl)benzotriazoles and N-Cbz-dipeptidoylbenzotriazoles to provide arginine LL-dipeptides 9a-e, 11a-d; LLL-tripeptides 18a-c, 20; and diastereomeric mixtures (9b+9b′), (9c+9c′), (11b+11b′) and (18c+18c′) [compound numbers written within parentheses represent a diastereomeric mixture or racemate; compound numbers without parentheses represent an achiral compound or a single enantiomer] by extension at the N-terminus of arginine, in isolated yields of 66-95% with complete retention of chirality as evidenced by NMR and HPLC analysis. Arginine LL-dipeptides 15a-d were synthesized by extension at the C-terminus of arginine in isolated yield of 66-80%, using benzotriazole activated arginine L-ωNO2-Arg-Bt, 13. Our methodology has also been used to synthesize the protected RGD peptide (Cbz α-L-ωNO2-Arg-Gly-L-Asp-(OH) 2) 21.

Cathepsin B-sensitive dipeptide prodrugs. 1. A model study of structural requirements for efficient release of doxorubicin

A series of lysosomal protease-sensitive peptides attached to doxorubicin (DOX) was prepared as model substrates for internalizing anticancer immunoconjugates and potential antimetastasis prodrugs. Rates of cathepsin B-mediated release of free drug was measured for each, and human plasma stabilities for representative examples.