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
• Article Data: 15

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

General Description

METHYL (S)-3-BOC-AMINOBUTYRATE is a chemical compound with the molecular formula C11H21NO4. It is a derivative of the amino acid valine and is commonly used as a building block in organic synthesis. METHYL (S)-3-BOC-AMINOBUTYRATE is a methyl ester of (S)-3-BOC-aminobutyric acid, which is a protected form of the amino acid. It is used in the production of peptides and pharmaceuticals, as well as in the study of biochemical pathways and drug development. Additionally, it is known for its ability to act as a neurotransmitter and its potential as a drug target for 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

• 24424-99-5 di-tert-butyl dicarbonate 
• 173143-75-4 (2S,3S)-1-Benzyl-3-methyl-aziridine-2-carboxylic acid methyl ester 
• 631914-55-1 Boc-L-Ala-Cl 
• 15761-38-3 L-N-Boc-Ala 
• 74-88-4 methyl iodide 
• 172695-22-6 (2-cyano-1(S)-methylethyl)carbamic acid, 1,1-dimethylethyl ester 
• 84765-24-2 (S)-O-(p-tolylsulfonyl)-N-(tert-butyloxycarbonyl)-1-hydroxy-2-aminopropane 
• 79069-13-9 (S)-2-t-butoxycarbonylaminopropan-1-ol 
• 158851-30-0 (S)-3-tert-butoxycarbonylaminobutyric acid 
• 67-56-1 methanol 
• 18107-18-1 diazomethyl-trimethyl-silane 
• 154079-54-6 (2S,3S)-3-tert-butoxycarbonylamino-1,2-butanediol 
• 106539-36-0 tert-butyl N-[(2S)-4-hydroxybutan-2-yl]carbamate 
• 115378-33-1 (-)-tert-butyl [(1S)-1-methylprop-2-en-1-yl]carbamate 

Downstream Products

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

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.

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

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.

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.