1114-55-2

Basic information

• Product Name: N-Acetyl-L-leucine ethyl ester
• Synonyms: (2S)-2-(Acetylamino)-4-methylvaleric acid ethyl ester;CVLYKMBNKKBAHO-VIFPVBQESA-N
• CAS NO: 1114-55-2
• Molecular Formula: C10H19 N O3
• Molecular Weight: 201.2628
• Mol File: 1114-55-2.mol

Chemical Properties

• Boiling Point: 307.7°Cat760mmHg
• Flash Point: 139.9°C
• Appearance: /
• Density: 0.987g/cm³
• Vapor Pressure: 0.000711mmHg at 25°C
• Refractive Index: 1.439
• CAS DataBase Reference: N-Acetyl-L-leucine ethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: N-Acetyl-L-leucine ethyl ester(1114-55-2)
• EPA Substance Registry System: N-Acetyl-L-leucine ethyl ester(1114-55-2)

Safety Data

• Hazardous Substances Data: 1114-55-2(Hazardous Substances Data)

Usage

Uses

Used in Nutritional Supplements:
N-Acetyl-L-leucine ethyl ester is used as a nutritional supplement for supporting muscle growth and recovery. It is valued for its anti-fatigue and anti-catabolic properties, making it popular among athletes and bodybuilders to improve physical performance and endurance.
Used in Pharmaceutical Research:
N-Acetyl-L-leucine ethyl ester is being explored for its potential therapeutic benefits in neurological disorders and cognitive function. Its role in these areas is currently under investigation, with the aim of understanding its mechanisms of action and potential side effects for future clinical applications.

InChI:InChI=1/C10H19NO3/c1-5-14-10(13)9(6-7(2)3)11-8(4)12/h7,9H,5-6H2,1-4H3,(H,11,12)

Upstream product

• 61-90-5 L-leucine 
• 4071-36-7 ethyl N-acetyl-leucinate 
• 108-24-7 acetic anhydride 
• 2743-40-0 L-leucine ethyl ester hydrochloride 
• 2743-60-4 L-Leucine ethyl ester 
• 75-36-5 acetyl chloride 

Relevant articles and documents

ROUTES TO OPTICALLY ACTIVE ELECTRON-RICH OLEFINS (L*2) AND SOME DERIVED CARBENEMETAL COMPLEXES; X-RAY STRUCTURES OF *)(NO)(PPh3)> AND cis-*)> *=, L'*=, COD = 1,5-C8H12>

Optically active electron-rich olefins L2* are obtained from readily available chiral starting materials , and are converted into carbenemetal (RhI or CoI) complexes with retention of optical integrity.

Competitive formation of 10- and 7-membered hydrogen-bonded rings of proline-containing model peptides

Intramolecularly hydrogen-bonded structures of proline-containing model peptides with a sequence of N-tert-butoxycarbonyl-prolyl-Xaa-NHCH3 [Xaa = Gly (glycyl), Ala (alanyl), Phe (phenylalanyl), Leu (leucyl), Ile (isoleucyl), and Val (valyl)] were studied by proton nuclear magnetic resonance and infrared spectroscopy. Variation of chemical shifts of amide protons with composition change of DMSO-d6/CDCl3 mixed solvents were found to be a good measure of intramolecular hydrogen bonding of peptides in CDCl3 solution. It has been shown that 10- and 7-membered hydrogen-bonded rings, which should have the β- and γ-turn like structures in proteins, respectively, form competitively with each other. It is suggested that the equilibrium between the two hydrogen-bonded rings is determined by steric hindrance due to a side chain of the Xaa residue. Free energies for formation of the 10- and 7-membered hydrogen-bonded rings, ΔG10 and ΔG7, were estimated from the solvent composition-dependent change of the chemical shifts. A good correlation between ΔG10 and the occurrence frequencies of residues Xaa at the (i + 2)th position for the β-turns in proteins has been found.