79722-10-4

Upstream product

• 13734-41-3 t-Boc-L-valine 
• 622-33-3 N-benzyloxyamine 
• 2687-43-6 O-benzylhydoxylamine hydrochloride 

Downstream Products

• 79722-16-0 [(S)-1-(Benzyloxy-methyl-carbamoyl)-2-methyl-propyl]-carbamic acid tert-butyl ester 

Relevant academic research and scientific papers

Transition-Metal-Free Synthesis of N-Aryl Hydroxamic Acids via Insertion of Arynes

An efficient and transition-metal-free N-arylation of amides via the insertion of arynes into the N-H bonds in the N-alkoxy amides is described. A variety of the reactive functional groups including the reactive aldehyde carbonyl group, furan ring, carbon-carbon double bonds, and free N-H bond of indole are found to be compatible with this process. In particular, the protocol is applicable in the synthesis of structurally diverse N-aryl hydroxamates and hydroxamic acids derived from N-protecting amino acids and peptides. In the presence of multiple amide N-H bonds, the N-arylation reaction can proceed selectively in the N-H bonds of terminal N-OBn amides giving rise to the desired N-aryl hydroxamates.

N-[(diphenoxyphosphoryl)oxy]-2-phenyl-1H-benzimidazole as a versatile reagent for synthesis O-alkylhydroxamic acids

(Chemical Equation Presented) Highly efficient reagent, N-[(diphenoxyphosphoryl)oxy]-2-phenyl-1H-benzimidazole was synthesized and its applicability was demonstrated for the synthesis of O-alkyl hydroxamic acids. The efficiency of the reagent was evaluate

Design, synthesis and utilization of a novel coupling reagent for the preparation of O-alkyl hydroxamic acids

An efficient novel reagent, phosphoric acid diethyl ester 2-phenyl-benzimidazol-1-yl ester, was designed, and synthesized and its applicability was demonstrated for the preparation of O-alkyl hydroxamic acids. The O-alkyl hydroxamic acids of N-protected a

Solution/solid-phase synthesis of partially modified retro- and retro-inverso-ψ[NHCH(CF3)]-peptidyl hydroxamates and their evaluation as MMP-9 inhibitors

The synthesis of a novel family of partially modified (PM) retro-and retro-inverso-peptidyl hydroxamates, each incorporating a [CH(CF3)CH2CO] unit as a surrogate for the conventional malonyl group, has been accomplished both in solution and in solid phase. The key step is the Michael-type N-addition of free or polymer-bound α-amino hydroxamates to 3-[(E)-enoyl]-1,3-oxazolidin-2-ones, which takes place in high yields, although with low stereocontrol. This method is suitable for the preparation of combinatorial libraries of PM retro-ψNHCH(CF3)]-peptidyl hydroxamates for screening as metalloprotease inhibitors. A number of tri- and tetrapeptidyl hydroxamates were indeed obtained either in diastereomerically pure form by solution-phase synthesis followed by chromatographic purification, or as mixtures of two epimers by solid-phase synthesis and release from the resin. X-ray diffraction of a Tfm-retropeptidyl hydroxamate showed an interesting turn-like conformation with an intramolecularly hydrogen-bonded nine-membered ring, and a nearly planar geometry of the NH group bound to the CH(CF3) group. Three retro-peptidyl hydroxamates were submitted to bioassays, and displayed the capacity to reduce MMP-9 (Gelatinase B) gelatinolytic activity.

Solution/solid-phase synthesis of partially modified retro-ψ[NHCH(CF3)]-peptidyl hydroxamates

The synthesis of a novel family of partially-modified (PM) retropeptidyl hydroxamates incorporating a [CH(CF3)CH2CO] unit as a surrogate of the conventional malonyl group, has been accomplished both in solution and in solid-phase. The key step is the Michael-type N-addition of free or polymer bound α-amino hydroxamates to 3-(E-enoyl)-1,3-oxazolidin-2-ones, which takes place very effectively, although with low stereocontrol. A number of tri- and tetra-peptidyl hydroxamates were obtained either in diastereomerically pure form (by solution-phase synthesis, after chromatographic purification), or as mixtures of two epimers in very good chemical purity (by solid-phase, after release from the resin), demonstrating that this method is suitable for preparing combinatorial libraries of PM retro-ψ[NHCH(CF3)]-peptidyl hydroxamates for screening as metalloprotease inhibitors.