2443-71-2

Upstream product

• 119153-86-5 C₁₆H₂₁NO₆ 
• 501-53-1 benzyl chloroformate 
• 134306-34-6 N-(Benzyloxycarbonyl)valine methyl ester 
• 1149-26-4 N-benzyloxycarbonylvaline 
• 119706-21-7 2-(benzhydrylamino)-2-oxoethyl ((benzyloxy)carbonyl)-L-valinate 
• 5276-76-6 4-nitrobenzyl ((benzyloxy)carbonyl)-L-valinate 
• 238400-05-0 2-hydroxyethyl ((benzyloxy)carbonyl)-L-valinate 
• 73504-31-1 benzyloxycarbonylamino 3-butyric acid benzyl ester 
• 42417-65-2 Z-MeVal-OH 
• 6306-52-1 L-valine methylester hydrochloride 
• 17498-50-9 L-valine hydrochloride 
• 67436-18-4 N-benzyloxycarbonyl-S-valine methyl ester 
• 1149-26-4 (S)-N-(benzyloxycarbonyl)valine 
• 72-18-4 L-valine 

Downstream Products

• 439916-77-5 [(S)-1-(1,3-Dioxo-1,3-dihydro-isoindol-2-ylcarbamoyl)-2-methyl-propyl]-carbamic acid benzyl ester 
• 646532-78-7 Cbz-Val-NHNHCH₂COO-t-Bu 
• 261729-63-9 1-(Cbz-valyl)-3,5-dimethylpyrazole 
• 1352815-88-3 C₂₅H₂₃N₃O₅ 
• 93788-22-8 (R,R)-bis(N-benzyloxycarbonylvalyl)diaza-18-crown-6 

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.

An efficient, stereocontrolled and versatile synthetic route to bicyclic partially saturated privileged scaffolds

Herein, we describe the development of a simple, high yielding and stereocontrolled strategy for the synthesis of a series of triazolopiperazines and other biologically relevant fused scaffolds from optically active amino acids. This route was applied to the synthesis of 22 scaffolds containing new, previously inaccessible vectors and used to access a novel analogue of ganaplacide.

FUMAGILLOL COMPOUNDS AND METHODS OF MAKING AND USING SAME

Disclosed herein, in part, are fumagillol compounds and methods of use in treating medical disorders, such as obesity. Pharmaceutical compositions and methods of making fumagillol compounds are provided. The compounds are contemplated to have activity against methionyl aminopeptidase 2.

PEPTIDOMIMETIC COMPOUNDS AND ANTIBODY-DRUG CONJUGATES THEREOF

This invention relates to peptidomimetic linkers and anti-body drug conjugates thereof, to pharmaceutical compositions containing them, and to their use in therapy for the prevention or treatment of cancer.

Carbonylhydrazide-based molecular tongs inhibit wild-type and mutated HIV-1 protease dimerization

We have designed and synthesized new molecular tongs based on a rigid naphthalene scaffold and evaluated their antidimer activity on HIV-1 protease (PR). We inserted carbonylhydrazide and oligohydrazide (azatide) fragments into their peptidomimetic arms t

A favorable, narrow, δh Hansen-parameter domain for gelation of low-molecular-weight amino acid derivatives

In recent years, the design of new low-molecular-weight gelators (LMWGs) has attracted considerable attention because of the interesting supramolecular architectures as well as industrial applications. In this context, the role of the organic solvent in d

Combinatorial synthesis of 3,5-Dimethylene substituted 1,2,4-Triazoles

Combinatorial cyclizations of imidates and hydrazides with methylene linked R groups, generated from the corresponding nitriles and carboxylic acids, respectively, provided a large library of 3,5-dimethylene substituted 1,2,4- trizoles. 2011 Bentham Science Publishers Ltd.

Design, synthesis, and evaluation of aza-peptide Michael acceptors as selective and potent inhibitors of caspases-2, -3, -6, -7, -8, -9, and -10

Aza-peptide Michael acceptors are a novel class of inhibitors that are potent and specific for caspases-2, -3, -6, -7, -8, -9, and -10. The second-order rate constants are in the order of 106 M-1 s-1. The aza-peptide Michael acceptor inhibitor 18t (Cbz-Asp-Glu-Val-AAsp-trans-CH=CH-CON(CH2-1-Naphth)2 is the most potent compound and it inhibits caspase-3 with a k2 value of 5620000 M-1 s-1. The inhibitor 18t is 13700, 190, 6.4, 594, 37500, and 173-fold more selective for caspase-3 over caspases-2, -6, -7, -8, -9, and -10, respectively. Aza-peptide Michael acceptors designed with caspase specific sequences are selective and do not show any cross reactivity with clan CA cysteine proteases such as papain, cathepsin B, and calpains. High-resolution crystal structures of caspase-3 and caspase-8 in complex with aza-peptide Michael acceptor inhibitors demonstrate the nucleophilic attack on C2 and provide insight into the selectivity and potency of the inhibitors with respect to the P1′ moiety.

Fast and convenient synthesis of α-N-protected amino acid hydrazides

A fast, simple and convenient synthesis of α-N-protected amino acid hydrazides is reported. The procedure involves the reaction between hydrazine monohydrate and the mixed anhydride obtained from an α-N-protected amino acid and ethyl chloroformate. When m

Design, Synthesis, and Evaluation of Aza-Peptide Epoxides as Selective and Potent Inhibitors of Caspases-1, -3, -6, and -8

Aza-peptide epoxides, a novel class of irreversible protease inhibitors, are specific for the clan CD cysteine proteases. Aza-peptide epoxides with an aza-Asp residue at P1 are excellent irreversible inhibitors of caspases-1, -3, -6, and -8 with second-order inhibition rates up to 1 910 000 M-1 s-1. In general, the order of reactivity of aza-peptide epoxides is S,S > R,R > trans > cis. Interestingly, some of the R,R epoxides while being less potent are actually more selective than the S,S epoxides. Our aza-peptide epoxides designed for caspases are stable, potent, and specific inhibitors, as they show little to no inhibition of other proteases such as the aspartyl proteases porcine pepsin, human cathepsin D, plasmepsin 2 from P. falciparum, HIV-1 protease, and the secreted aspartic proteinase 2 (SAP-2) from Candida albicans; the serine proteases granzyme B and α-chymotrypsin; and the cysteine proteases cathepsin B and papain (clan CA), and legumain (clan CD).