106539-14-4

Basic information

• Product Name: METHYL (S)-3-BOC-AMINOBUTYRATE
• Synonyms: METHYL (S)-3-BOC-AMINOBUTYRATE;Zinc04202785;(S)-methyl 3-(tert-butoxycarbonyl)butanoate
• CAS NO: 106539-14-4
• Molecular Formula: C₁₀H₁₉NO₄
• Molecular Weight: 217.26
• Product Categories: pharmacetical
• Mol File: 106539-14-4.mol

Chemical Properties

• Boiling Point: 302.8°Cat760mmHg
• Flash Point: 136.9°C
• Appearance: /
• Density: 1.035g/cm³
• Vapor Pressure: 0.00097mmHg at 25°C
• Refractive Index: 1.441
• CAS DataBase Reference: METHYL (S)-3-BOC-AMINOBUTYRATE(CAS DataBase Reference)
• NIST Chemistry Reference: METHYL (S)-3-BOC-AMINOBUTYRATE(106539-14-4)
• EPA Substance Registry System: METHYL (S)-3-BOC-AMINOBUTYRATE(106539-14-4)

Safety Data

• Hazardous Substances Data: 106539-14-4(Hazardous Substances Data)

Usage

Uses

Used in Organic Synthesis:
METHYL (S)-3-BOC-AMINOBUTYRATE is used as a building block in organic synthesis for the creation of various chemical compounds. Its protected form allows for controlled reactions and the synthesis of complex organic molecules.
Used in Pharmaceutical Production:
In the pharmaceutical industry, METHYL (S)-3-BOC-AMINOBUTYRATE is utilized as a key component in the development and production of drugs. Its role in the synthesis of peptides and pharmaceuticals contributes to the advancement of new medications and therapies.
Used in Biochemical Pathway Research:
METHYL (S)-3-BOC-AMINOBUTYRATE is employed in the study of biochemical pathways to understand its role in biological systems. This research aids in the discovery of new mechanisms and potential therapeutic targets.
Used in Drug Development:
METHYL (S)-3-BOC-AMINOBUTYRATE is used in drug development for its potential as a drug target in the treatment of neurological disorders. Its neurotransmitter function and protective properties make it a valuable candidate for the development of new drugs targeting the nervous system.
Used in Neurotransmitter Research:
METHYL (S)-3-BOC-AMINOBUTYRATE is used as a neurotransmitter in research to explore its effects on the nervous system and its potential applications in treating neurological conditions. Understanding its role as a neurotransmitter can lead to the development of novel treatments for various neurological disorders.

InChI:InChI=1/C10H19NO4/c1-7(6-8(12)14-5)11-9(13)15-10(2,3)4/h7H,6H2,1-5H3,(H,11,13)/t7-/m0/s1

Upstream product

• 186581-53-3 diazomethane 
• 158851-30-0 (S)-3-tert-butoxycarbonylaminobutyric acid 
• 67-56-1 methanol 
• 67919-80-6 (S)-3-[(tert-butoxy)carbonylamino]-1-diazobutan-2-one 
• 24424-99-5 di-tert-butyl dicarbonate 
• 6078-06-4 (S)-methyl 3-aminobutanoate 
• 173143-75-4 (2S,3S)-1-Benzyl-3-methyl-aziridine-2-carboxylic acid methyl ester 
• 78-83-1 2-methyl-propan-1-ol 
• 163254-35-1 methyl 3-((tert-butoxycarbonyl)amino)butanoate 
• 4248-19-5 tert-butyl carbazate 
• 105-45-3 acetoacetic acid methyl ester 
• 15761-38-3 L-N-Boc-Ala 
• 109208-68-6 Boc-Ala-O-COO-isoBu 
• 115378-33-1 (-)-tert-butyl [(1S)-1-methylprop-2-en-1-yl]carbamate 

Downstream Products

• 106539-36-0 tert-butyl N-[(2S)-4-hydroxybutan-2-yl]carbamate 
• 118173-26-5 (S)-3-tert-butoxycarbonylamino-butanal 
• 190598-38-0 (2S,3S)-3-tert-Butoxycarbonylamino-2-phenylselanyl-butyric acid 
• 190598-41-5 (S)-1-((2S,3S)-3-tert-Butoxycarbonylamino-2-phenylselanyl-butyryl)-pyrrolidine-2-carboxylic acid 2-trimethylsilanyl-ethyl ester 
• 6078-06-4 (S)-methyl 3-aminobutanoate 
• 139243-55-3 (S)-3-aminobutanoic acid methyl ester hydrochloride 
• 186494-09-7 (2S,3S)-3-([(tert-butoxy)carbonyl]amino)-2-methylbutanoicacid 

Relevant articles and documents

Thermodynamic Scale of β-Amino Acid Residue Propensities for an α-Helix-like Conformation

A thiol-thioester exchange system has been used to measure the propensities of diverse β-amino acid residues to participate in an α-helix-like conformation. These measurements depend on formation of a parallel coiled-coil tertiary structure when two peptide segments become linked by thioester formation. One peptide segment contains a "guest" site that accommodates diverse β residues and is distal to the coiled-coil interface. We find that helix propensity is influenced by side chain placement within the β residue [β3 (side chain adjacent to nitrogen) slightly favored relative to β2 (side chain adjacent to carbonyl)]. The previously recognized helix stabilization resulting from five-membered ring incorporation is quantified. These results are significant because so few quantitative thermodynamic measurements have been reported for α/β-peptide folding.

On the enantioselective hydrogenation of isomeric β-acylamido β-alkylacrylates with chiral Rh(I) complexes - Comparison of phosphine ligands and substrates

The rhodium(I)-catalyzed enantioselective hydrogenation of E- and Z-configured β-acylamido β-alkylacrylates as well as of isomeric mixtures has been investigated. As ligands 1,2-bisphospholanes like DuPHOS, BPE and Me4-BASPHOS have been tested,

Enzymatic resolution of N-protected-β3-amino methyl esters, using lipase B from Candida antarctica

Racemic β3-amino methyl esters bearing the amine function protected with Bz, Cbz, Boc, Fmoc and as aminobenzamide, were resolved by enantiospecific transesterifications catalyzed by lipase B from Candida antarctica. The reactions proceeded with

1. Use of the Wolff Rearrangement of Diazo Ketones from Amino Acids as a Synthetic Method for the Formation of Oligonucleo-peptides: A Novel Approach to Chimeric Biomolecules

Photolysis and Ag-benzoate-catalyzed decomposition of the diazo ketones 2 and 4 derived from Z-Ala-OH and Z-Ala-Ala-OH in the presence of oligonucleotide derivatives bearing at the 5′-terminus an NH2 instead of the OH group, or an aminohexyl phosphate group lead to Z-protected 3-aminobutanoyl and to Z-Ala-β-HAla derivatives, respectively (conjugates 12, 13, and 17-23, Schemes 3-5). In solution, this amide-forming acylation reaction could be realized only with oligomers containing up to 8 unprotected nucleotide building blocks (Schemes 3 and 4). With the analogous polymer-bound and protected oligonucleotide derivatives as amino nucleophiles, excellent yields were obtained with all chain lengths tested (up to 15mer, Scheme 5). The products were purified by reversed-phase HPLC and characterized by MALDI-TOF mass spectrometry (Figs. 2-4, Table 2) and by capillary gel electrophoresis (Fig. 2).

Modulation of the Passive Permeability of Semipeptidic Macrocycles: N- And C-Methylations Fine-Tune Conformation and Properties

Incorporating small modifications to peptidic macrocycles can have a major influence on their properties. For instance, N-methylation has been shown to impact permeability. A better understanding of the relationship between permeability and structure is of key importance as peptidic drugs are often associated with unfavorable pharmacokinetic profiles. Starting from a semipeptidic macrocycle backbone composed of a tripeptide tethered head-to-tail with an alkyl linker, we investigated two small changes: peptide-to-peptoid substitution and various methyl placements on the nonpeptidic linker. Implementing these changes in parallel, we created a collection of 36 compounds. Their permeability was then assessed in parallel artificial membrane permeability assay (PAMPA) and Caco-2 assays. Our results show a systematic improvement in permeability associated with one peptoid position in the cycle, while the influence of methyl substitution varies on a case-by-case basis. Using a combination of molecular dynamics simulations and NMR measurements, we offer hypotheses to explain such behavior.

Synthesis and evaluation of chiral β-amino acid-based low-molecular-weight organogelators possessing a methyl/trifluoromethyl side chain

The synthesis and gelation properties of chiral β-amino acid-based low-molecular-weight organogelators, possessing methyl/trifluoromethyl side chains, are reported. The structure of the side chain and chirality were found to be important parameters affecting the gelation ability. The pure enantiomer of the trifluoromethylated β-amino acid displayed good gelation properties due to the formation of fibrillar networks, driven by enhanced amide hydrogen bonding. An investigation of the effects of the alkyl chain length showed that longer alkyl chain improved the gelation ability, yet the same supramolecular structure was observed in all, as well as an odd-even effect in both the melting points and Tg values.

PYRROLO [2, 3 - B] PYRAZINE - 7 - CARBOXAMIDE DERIVATIVES AND THEIR USE AS JAK AND SYK INHIBITORS

The present invention relates to the use of novel pyrrolopyrazine derivatives of Formula (I), wherein the variables Q and R, R2, and R3 are defined as described herein, which inhibit JAK and SYK and are useful for the treatment of auto-immune and inflammatory diseases.

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.