197006-14-7

Basic information

• Product Name: 4-BOC-(R)-AMINO-5-METHYL HEXANOIC ACID
• Synonyms: 4-BOC-(R)-AMINO-5-METHYL HEXANOIC ACID;4-T-BUTOXYCARBONYL-(R)-AMINO-5-METHYL HEPTANOIC ACID;BOC-VAL-[C*(CH2)2]OH;BOC-GAMMAVAL;BOC-GAMMA-VAL-OH;(R)-BOC-4-AMINO-5-METHYL-HEXANOIC ACID;N-T-BUTOXYCARBONYL-GAMMA-L-VALINE
• CAS NO: 197006-14-7
• Molecular Formula: C₁₂H₂₃NO₄
• Molecular Weight: 245.32
• Mol File: 197006-14-7.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: 4-BOC-(R)-AMINO-5-METHYL HEXANOIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: 4-BOC-(R)-AMINO-5-METHYL HEXANOIC ACID(197006-14-7)
• EPA Substance Registry System: 4-BOC-(R)-AMINO-5-METHYL HEXANOIC ACID(197006-14-7)

Safety Data

• Hazardous Substances Data: 197006-14-7(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Upstream product

• 2026-48-4 (S)-valinol 
• 62596-65-0 (2S)-2-isopropyl-1-[(4-methylphenyl)sulfonyl]aziridine 
• 72-18-4 L-valine 
• 79069-14-0 (S)-2-<(tert-butoxycarbonyl)amino>-3-methylbutan-1-ol 
• 79069-51-5 (S)-N-tert-butoxycarbonylvalinal 
• 197006-06-7 tert-butyl (R)-(1-(2,2-dimethyl-4,6-dioxo-1,3-dioxan-5-yl)-3-methylbutan-2-yl)carbam ate 
• 13734-41-3 t-Boc-L-valine 
• 207924-96-7 (4S)-tert-butoxycarbonylamino-5-methyl-hex-(2E)-enoic acid methyl ester 
• 58561-04-9 N-tert-butoxycarbonyl-L-valine methyl ester 
• 207924-87-6 tert-butyl (1R)-1-isopropyl-4-diazo-3-oxobutylcarbamate 
• 147778-57-2 (4R)-tert-butoxycarbonylamino-5-methyl-hexanoic acid methyl ester 
• 147778-56-1 tert-butyl (R)-2-isopropyl-5-oxopyrrolidine-1-carboxylate 

Downstream Products

• 207925-00-6 (R)-4-[(S)-4-((R)-4-{(R)-4-[(S)-4-((R)-4-tert-Butoxycarbonylamino-5-methyl-hexanoylamino)-pentanoylamino]-6-methyl-heptanoylamino}-5-methyl-hexanoylamino)-pentanoylamino]-6-methyl-heptanoic acid benzyl ester 
• 207924-98-9 (R)-4-[(S)-4-((R)-4-tert-Butoxycarbonylamino-5-methyl-hexanoylamino)-pentanoylamino]-6-methyl-heptanoic acid benzyl ester 

Relevant articles and documents

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Structural characterization of folded pentapeptides containing centrally positioned β(R)Val, γ(R)Val and γ(S)Val residues

A cylindrical pore of ～7.5 diameter containing a one-dimensional water wire, within the confines of a hydrophobic channel lined with the valine side chain, has been observed in crystals of the peptide Boc-d-Pro-Aib-Val-Aib-Val- OMe (1) (Raghavender et al., 2009, 2010). The synthesis and structural characterization in crystals of three backbone homologated analogues Boc-d-Pro-Aib-β3(R)Val-Aib-Val-OMe (2), Boc-d-Pro-Aib- γ4(R)Val-Aib-Val-OMe (3), Boc-d-Pro-Aib-γ4(S) Val-Aib-Val-OMe (4) are described. Crystal structures of peptides 2, 3 and 4 reveal close-packed arrangements in which no pore was formed. In peptides 2 and 3 the N-terminus d-Pro-Aib segment adopted conformations closely related to Type II′ β-turns, while residues 2-4 form one turn of an αβ right-handed C11 helix in 2 and an αγ C12 helix in 3. In peptide 4, a continuous left-handed helical structure was observed with the d-Pro-Aib segment forming a Type III′ β-turn, followed by one turn of a left-handed αγ C12 helix.

The natural product hybrid of Syringolin A and Glidobactin A synergizes proteasome inhibition potency with subsite selectivity

The preparation of a Syringolin A/Glidobactin A hybrid (SylA-GlbA) consisting of a SylA macrocycle connected to the GlbA side chain and its potent proteasome targeting of all three proteasomal subsites is reported. The influence of the syrbactin macrocycle moiety on subsite selectivity is demonstrated.

Consequences of isostructural main-chain modifications for the design of antimicrobial foldamers: Helical mimics of host-defense peptides based on a heterogeneous amide/urea backbone

"Chemical Equation Presented" Fraternal twins: Oligoureas and Y-peptides are isosteric, quasi-isostructural helical foldamers endowed with distinct blomolecular recognition properties. Combination of the two backbones to generate urea/amide hybrids (see picture) was found to give more potent yet less cytotoxic antimicrobial helical foldamers.

2-AMINO-3,4-DIHYDRO-PYRIDO[3,4-D]PYRIMIDINE DERIVATIVES USEFUL AS INHIBITORS OF BETA-SECRETASE (BACE)

The present invention is directed to 2-amino-3,4-dihydro-pyrido[3,4-d]pyrimidine derivatives of formula (I), pharmaceutical compositions containing them and their use in the treatment of Alzheimer's disease (AD) and related disorders. The compounds of the invention are inhibitors of β-site cleaving enzyme and BACE, BACE1, Asp2 and memapsin2.

MACROCYCLE DERIVATIVES USEFUL AS INHIBITORS OF beta-SECRETASE (BACE)

The present invention is directed to macrocycle derivatives, pharmaceutical compositions containing them and their use in the treatment of Alzheimer's disease (AD) and related disorders. The compounds of the invention are inhibitors of β-secretase, also known as β-site cleaving enzyme and BACE, BACE1, Asp2 and memapsin2.

NOVEL 2-AMINO-QUINAZOLINE DERIVATIVES USEFUL AS INHIBITORS OF β-SECRETASE (BACE)

The present invention is directed to novel 2-amino-3, 4-dihydro-quinazoline derivatives, pharmaceutical compositions containing them and their use in the treatment of Alzheimer's disease (AD) and related disorders. The compounds of the invention are inhibitors of P-secretase, also known as n-site cleaving enzyme and BACE.

Trifluoroacetic acid-mediated intramolecular formal N-H insertion reactions with amino-α-diazoketones: A facile and efficient synthesis of optically pure pyrrolidinones and piperidinones

Trifluoroacetic acid (TFA) was found to promote intramolecular formal N-H insertion reactions. Upon treatment with TFA, optically pure N-Boc-β′-amino-α-diazoketones (5a-c) and N-Boc-γ′-amino-α-diazoketones (10a-d) can be converted, with retention of chira

γ-Peptides Forming More Stable Secondary Structures than α-Peptides: Synthesis and Helical NMR-Solution Structure of the γ-Hexapeptide Analog of H-(Val-Ala-Leu)2-OH

For a comparison with the corresponding α- and β-hexapeptides H-(Val-Ala-Leu)2-OH (A) and H-(β-HVal-β-HAla-β-HLeu)2-OH (B), we have now prepared the corresponding γ-hexapeptide 1 built from the homochirally similar (S)-4-aminobutanoic acid, (R)-4-amino-5-methylhexanoic acid, and (R)-4-amino-6-methylheptanoic acid. The precursors were prepared either by double Arndt-Eistert homologation of the protected amino acids Boc-Val-OH, Boc-Ala-OH, and Boc-Leu-OH (Schemes 1 and 2), or by the superior route involving olefination/hydrogenation of the corresponding aldehydes (Boc-valinal, Boc-alaninal, and Boc-leucinal; Scheme 3). Conventional peptide-coupling methodology (EDC/HOBt) furnished the γ-hexapeptide 1 (through the intermediate γ-di- and γ-tripeptide derivatives 9-11). Analysis of NMR measurements in (D5)pyridine and CD3OH solution (COSY, TOCSY, HSQC, HMBC, ROESY) reveals that the γ-hexapeptide 1 adopts a right-handed helical structure ((P)-2.61 helix of ca. 5-A pitch, containing 14-membered H-bonded rings) which is to be compared with the left-handed helix of the corresponding β-peptide B ((M)-31 helix of 5-A pitch, 14-membered H-bonded rings) and with the familiar right-handed, so-called α-helix of α-peptides ((P)-3.61 helix of 5.4-A pitch, 13-membered rings). Like the helix sense, the helix dipole reverses when going from α- (N C) to β- (C N) to γ-peptides (N C). The surprising difference between the natural α-, and the analogous β- and γ-peptides is that the helix stability increases upon homologation of the residues.

Facile stereoselective synthesis of γ-substituted γ-amino acids from the corresponding α-amino acids

A facile stereoselective method for the synthesis of γ-substituted, γ-amino acids from α-amino acids was developed. The key step of the procedure is complete reduction of the keto functionality of α-amino acyl Meldrum's acid by sodium acetoxyborohydride. The resulting amino alkyl Meldrum's acid undergoes thermal decarboxylative ring closure to a 5-substituted pyrrolidinone which yields the corresponding γ-amino acid after basic hydrolysis. The overall yield of the procedure ranges from 40 to 65%.