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
• Article Data: 4

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

General Description

N-Acetyl-L-leucine ethyl ester is a chemical compound that is derived from the amino acid leucine. It is a modified form of leucine that has been acetylated and esterified with ethyl alcohol. N-Acetyl-L-leucine ethyl ester is commonly used as a nutritional supplement to support muscle growth and recovery, as well as to improve physical performance and endurance. It is believed to have anti-fatigue and anti-catabolic properties, making it popular among athletes and bodybuilders. Research also suggests that N-Acetyl-L-leucine ethyl ester may have potential therapeutic benefits for neurological disorders and cognitive function. However, more studies are needed to fully understand its mechanisms of action and potential side effects.

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

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

Relevant articles and documents

The effects of salts on the free energies of nonpolar groups in model peptides.

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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.