2885-02-1

Basic information

• Product Name: (S)-Butyl 2-aMinopropanoate
• Synonyms: (S)-Butyl 2-aMinopropanoate;L-Ala-nbu;butyl (2S)-2-aminopropanoate
• CAS NO: 2885-02-1
• Molecular Formula: C₇H₁₅NO₂
• Molecular Weight: 145.1995
• Mol File: 2885-02-1.mol

Chemical Properties

• Boiling Point: 72-73 °C(Press: 10 Torr)
• Appearance: /
• Density: 0.957±0.06 g/cm3(Predicted)
• Storage Temp.: under inert gas (nitrogen or Argon) at 2–8 °C
• PKA: 7.81±0.29(Predicted)
• CAS DataBase Reference: (S)-Butyl 2-aMinopropanoate(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-Butyl 2-aMinopropanoate(2885-02-1)
• EPA Substance Registry System: (S)-Butyl 2-aMinopropanoate(2885-02-1)

Safety Data

• Hazardous Substances Data: 2885-02-1(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
(S)-Butyl 2-aminopropanoate is used as an active pharmaceutical ingredient for the development of various medications. Its unique chemical structure allows it to interact with biological systems, making it a valuable component in the formulation of drugs.
Used as a Flavoring Agent in the Food Industry:
(S)-Butyl 2-aminopropanoate is used as a flavor enhancer in the food industry due to its slightly sweet odor. It adds a pleasant taste to various food products, improving their overall flavor profile.
Used in Organic Synthesis:
(S)-Butyl 2-aminopropanoate serves as an intermediate in organic synthesis, contributing to the production of various chemical compounds. Its versatile chemical properties make it a valuable component in the synthesis of a wide range of products.
Used in Cosmetics and Personal Care Products:
(S)-Butyl 2-aminopropanoate is used in the manufacture of cosmetics and personal care products due to its mild and non-irritating nature. It can be incorporated into formulations to enhance the sensory experience and provide additional benefits to the end products.

Upstream product

• 1534344-81-4 Fmoc-Ala-OBu 
• 117402-81-0 n-butyl N-benzyloxycarbonylalaninoate 
• 56-41-7 L-alanin 
• 71-36-3 butan-1-ol 
• 10065-72-2 L-Alanine methyl ester 

Downstream Products

• 2749-11-3 (S)-Alaninol 
• 1442452-21-2 (2S)-2-(((perfluorophenoxy)(phenoxy)phosphoryl)amino)propionic acid butyl ester 
• 1375071-01-4 butyl N-[(S)-{[(4R,5R,7R,8R)-5-(2,4-dioxo-3,4-dihydro-pyrimidin-1(2H)-yl)-8-hydroxy-1,6-dioxaspiro[3.4]oct-7-yl]methoxy}(phenoxy)-phosphoryl]-L-alaninate 
• 1353757-51-3 (S,E)-n-butyl 2-methyl-2-(pyrrolidin-1-yl)-4-(p-toluenesulfonyl)but-3-enoate 
• 176239-88-6 (S)-N-(4-methyl-3-pentenyl)-N-tosylalanine butyl ester 
• 176239-76-2 (S)-N-benzyl-N-(4-methyl-3-pentenyl)alanine butyl ester 

Relevant articles and documents

Novel tenofovir mixed ester-amide prodrugs

The invention relates to novel tenofovir mixed ester-amide prodrugs or pharmaceutically acceptable salts thereof, a preparation method thereof, pharmaceutical compositions containing the prodrug compounds, and application of the prodrugs in preparation of drugs for treating virus infection such as hepatitis B virus (HBV) or human immunodeficiency virus (HIV) infection.

Supramolecular enantiomeric and structural differentiation of amino acid derivatives with achiral pillar[5]arene homologs

Complexation of achiral pillar[5]arenes with chiral amines induced strong circular dichroism (CD) signals. The CD responses differed drastically depending on the nature of the amino acid guest, and they significantly varied and part of them even inverted, upon increasing the length of the alkyl chains of the pillar[5]arenes guests. Accordingly, this tactic allowed for the unprecedented simultaneous enantiomeric and structural differentiation of α-amino esters with homologous molecular hosts.

A mild removal of Fmoc group using sodium azide

A mild method for effectively removing the fluorenylmethoxycarbonyl (Fmoc) group using sodium azide was developed. Without base, sodium azide completely deprotected Nα-Fmoc-amino acids in hours. The solvent-dependent conditions were carefully studied and then optimized by screening different sodium azide amounts and reaction temperatures. A variety of Fmoc-protected amino acids containing residues masked with different protecting groups were efficiently and selectively deprotected by the optimized reaction. Finally, a biologically significant hexapeptide, angiotensin IV, was successfully synthesized by solid phase peptide synthesis using the developed sodium azide method for all Fmoc removals. The base-free condition provides a complement method for Fmoc deprotection in peptide chemistry and modern organic synthesis. Graphical Abstract: [Figure not available: see fulltext.]

Asymmetric α-2-tosylethenylation of N,N-dialkyl-l-amino acid esters via the formation of non-racemic ammonium enolates

Asymmetric α-2-tosylethenylation of (S)-2-(pyrrolidin-1-yl)propanoic acid esters was shown to produce good yields with high enantioselectivities. The reaction proceeds via the formation of a non-racemic ammonium enolate without an external source of chirality.

Preparation of 2,3,4-trisubstituted piperidines by a formal hetero-ene reaction of amino acid derivatives

N-Benzyl- or N-tosyl-N-(4-methyl-3-pentenyl)amino aldehyde benzylimines, which are obtained from alanine, leucine, or phenylalanine methyl esters in five steps, can be cyclized diastereoselectively in the presence of Lewis acids to give 3-amino-2,4-dialkyl-substituted piperidines. The product distribution and diastereoselectivity depends on the type of Lewis acid and nitrogen-protecting group. Benzyl-protected imines give 2-alkyl-3-(benzylamino)-4-isopropenyl piperidines with FeCl3 and 2-alkyl-3-(benzylideneamino)-4-isopropylpiperidines with TiCl4. Tosyl-protected imines show a decreased level of selectivity. The relative configurations of the piperidines were established by NMR and X-ray crystal structure analyses. Iminium ion cyclization followed by two competitive ionic pathways, i.e. either proton elimination or hydride transfer are discussed for these reactions.

ENANTIOSELECTIVE HYDROLYSIS BY BAKER'S YEAST - II. ESTERS OF N-ACETYL AMINO ACIDS

D-N-Acetyl amino acid esters were obtained via enantioselective hydrolysis of their racemates by use of fermenting yeast.Evidence is given that proteinases are the enzymes involved.