5276-76-6

Upstream product

• 619-73-8 4-nitrobenzyl chloride 
• 1149-26-4 (S)-N-(benzyloxycarbonyl)valine 
• 100-11-8 1-bromomethyl-4-nitro-benzene 

Downstream Products

• 21760-98-5 L-valine benzyl ester 
• 2443-71-2 benzyl (S)-(1-hydrazineyl-3-methyl-1-oxobutan-2-yl)carbamate 
• 77313-52-1 Ac-Ser-Asp(OBzl)-Ala-Ala-Val-ONb 
• 77313-51-0 Boc-Asp(OBzl)-Ala-Ala-Val-ONb 
• 77313-53-2 Ac-Ser-Asp(OBzl)-Ala-Ala-Val-OH 
• 77313-50-9 Boc-Ala-Ala-Val-ONb 
• 40299-20-5 Boc-Ala-Val-ONb 
• 731746-19-3 H-Ala-Ala-Val-ONb 
• 769860-52-8 H-Ala-Val-ONb 
• 46925-27-3 L-valine p-nitrobenzyl ester 
• 21356-77-4 (S)-2-((S)-2-Benzyloxycarbonylamino-3-methyl-butyrylamino)-4-carbamoyl-butyric acid 4-nitro-benzyl ester 

Relevant academic research and scientific papers

An Atom-Economic Inverse Solid-Phase Peptide Synthesis Using Bn or BcM Esters of Amino Acids

An atom-economic N-to-C-directed solid-phase peptide synthesis is reported that uses benzyl (Bn) or (benzhydryl-carbamoyl)-methyl (BcM) esters of amino acids as the building blocks, which facilitate efficient hydrazinolysis, convenient conversion to acyl azide, and robust amidation with the next amino acid ester. This method is free of coupling reagents and free of protection on the side-chain OH, CO2H, CONH2, etc., therefore exhibiting a significantly improved atom economy compared to those of BOC- or Fmoc-based C-to-N-directed approaches.

Relaxing substrate specificity in antibody-catalyzed reactions: Enantioselective hydrolysis of N-Cbz-amino acid esters

For a catalytic antibody to be generally useful for organic synthetic chemistry, it must be able to accept a broad range of substrates, yet retain high selectivity. In this work, we propose a hapten design to endow antibody catalysts with two opposing qualities, such as high enantioselectivity and broad substrate specificity. Racemic hapten 2 induced two separate classes of catalytic antibodies to hydrolyze either the L- or D-isomers of N-Cbz-amino acid esters 1. In the kinetic resolution of racemic ester 9, antibodies 7G12 and 3G2 gave 96% ee of L-10 and 94% ee of D-10, respectively. In addition, antibody 7G12 displayed broad substrate specificity, hydrolyzing the L-esters of Ala (1a), Leu (1b), Norleu (1c), Met (1d), Phe (1e), Val (1f), and phenylglycine (1g) with high enantioselectivity. Antibody 3G2 also hydrolyzed the D-isomers of these esters without sacrificing the enantioselectivity. This observation suggests that the use of haptens that fit snugly into the antigen-combining site, and leave the linker moiety outside, is an effective approach for the generation of catalytic antibodies with high selectivity and broad substrate applicability.