115364-82-4

Basic information

• Product Name: (S)-tert-butyl (1-((benzyloxy)amino)-1-oxo-3-phenylpropan-2-yl)-carbamate
• Synonyms: (S)-tert-butyl (1-((benzyloxy)amino)-1-oxo-3-phenylpropan-2-yl)-carbamate
• CAS NO: 115364-82-4
• Molecular Weight: 370.448
• Mol File: 115364-82-4.mol

Chemical Properties

• CAS DataBase Reference: (S)-tert-butyl (1-((benzyloxy)amino)-1-oxo-3-phenylpropan-2-yl)-carbamate(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-tert-butyl (1-((benzyloxy)amino)-1-oxo-3-phenylpropan-2-yl)-carbamate(115364-82-4)
• EPA Substance Registry System: (S)-tert-butyl (1-((benzyloxy)amino)-1-oxo-3-phenylpropan-2-yl)-carbamate(115364-82-4)

Safety Data

• Hazardous Substances Data: 115364-82-4(Hazardous Substances Data)

Upstream product

• 622-33-3 N-benzyloxyamine 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 474890-08-9 1,1-dimethylethyl [(1S)-2-oxo-2-(2-oxo-3-oxazolidinyl)-1-(phenylmethyl)ethyl]carbamate 
• 2687-43-6 O-benzylhydoxylamine hydrochloride 

Downstream Products

• 58207-45-7 Phe-NH-O-CH₂-Ph 
• 115364-85-7 N-<2-(benzyloxycarbonyl)-1-oxoethyl>-L-phenylalanine N'-(benzyloxy)amide 
• 115364-55-1 (S)-N-(2-carboxy-1-oxoethyl)phenylalanine N'-hydroxyamide 
• 612815-61-9 [(S)-1-((S)-1-Benzyloxycarbamoyl-2-phenyl-ethylcarbamoyl)-2-hydroxy-ethyl]-carbamic acid tert-butyl ester 
• 58207-46-8 (S)-phenylalanine N'-(benzyloxy)amide trifluoroacetate 

Relevant articles and documents

A convenient method for the conversion of N-acyloxazolidinones to hydroxamic acids

(matrix presented) Treatment of N-acyloxazolidinones with hydroxylamines using samarium triflate as a Lewis acid provides the corresponding hydroxamic acids in 50-98% yields at room temperature. The conversion proceeds with high degree of chemoselectivity and without racemization of chiral centers α- to the acyl group.

Catalyst-Controlled Regiodivergent Synthesis of α/β-Dipeptide Derivatives via N-Allylic Alkylation of O-Alkyl Hydroxamates with MBH Carbonates

A controllable and regiodivergent N-allylation reaction involving readily available O-alkyl hydroxamates derived from natural α-amino acids has been developed, allowing regiospecific access to α/β-dipeptides containing α-unsaturated β-amino acids moieties in moderate to good yields. The regioselectivity could be conveniently switched by alternation of the catalysts and solvents.

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.

DERIVATIVES OF DOLASTATIN 10 AND USES THEREOF

Derivatives of dolastatin 10 and uses thereof, the structures of which are shown as formula I, II, III and IV are provided.

Synthesis of O-benzyl hydroxamates employing the sulfonate esters of N-hydroxybenzotriazole

The direct conversion of various carboxylic acids, that include sterically hindered amino acids and di-peptides, to O-benzyl hydroxamates is demonstrated using sulfonate esters of benzotriazoles under ambient and milder conditions without significant race

Solid-phase synthesis of conformationally constrained peptidomimetics based on a 3,6-disubstituted-1,4-diazepan-2,5-dione core

Starting from a Cl-trytyl linked hydroxylamine, a hydroxamic dipeptide having serine in the second position was prepared by using DMTMM as the coupling agent. Mitsunobu cyclization carried out under microwave heating gave very good yields of a 3,6-disubstituted-perhydro-diazepin-2,5-dione. This heterocycle can be used as a new platform for combinatorial chemistry or as a constraint to rigidify a small peptide.

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.

Direct synthesis of hydroxamates from carboxylic acids using 2-mercaptopyridone-1-oxide-based thiouronium salts

Tetrafluoroborate and hexafluorophosphate thiouronium salts derived from 2-mercaptopyridone-1-oxide and tetramethylurea (TOTT and HOTT) or N,N′-dimethylpropyleneurea (TODT and HODT) convert carboxylic acids to Weinreb amides and N-methoxy or N-benzoxyamides in high yields by reaction with N,O-dimethylhydroxylamine and O-methyl- or O-benzyl-hydroxylamine hydrochlorides, respectively, in the presence of triethylamine or DIEA.

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.

Retro-inverso concept applied to the complete inhibitors of enkephalin-degrading enzymes

Peptide retro-inverso modification was applied to the complete hydroxamate inhibitors of the three zinc metallopeptidases (neutral endopeptidase 24-11 (NEP, EC 3.4.24.11), aminopeptidase N (APN, EC 3.4.11.2), and a dipeptidylaminopeptidase (DAP) involved in the in vitro enkephalin degradation by brain tissues. Compounds corresponding to the general formula RN(OH)CO(CH2)(n)CH(CH2Ph)NHCOCH(R')COOH (n=0, 1) were synthesized. In the first series of inhibitors (n=0), the 'retro-inverso' modification induced a large decrease in inhibitory potency for NEP as compared to that of the parent compounds. In contrast, the presence of a methylene group between the hydroxamate and CHα in the second series (n=1) led to derivatives with inhibitory potencies in the nanomolar range, similar to their analogues with a natural amide bond. On the other hand, the retro-inverso modification led to a slight improvement in the inhibition of DAP and APN, in the first series of inhibitors, while the inverse result occurred in the second series. Thus, compounds containing an α-amino acid moiety in P'1 position behave as weak inhibitors of the three enzymes, with IC50 values in the micromolar range, and compounds bearing a β-amino acid moiety in the same position are more specific than the parent compounds for NEP inhibition.