4819-22-1

Basic information

• Product Name: N-Acetyl-L-isoleucine ethyl ester
• Synonyms: N-Acetyl-L-isoleucine ethyl ester;(2S,3S)-Ethyl 2-acetaMido-3-Methylpentanoate
• CAS NO: 4819-22-1
• Molecular Formula: C₁₀H₁₉NO₃
• Molecular Weight: 201.26
• Mol File: 4819-22-1.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: N-Acetyl-L-isoleucine ethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: N-Acetyl-L-isoleucine ethyl ester(4819-22-1)
• EPA Substance Registry System: N-Acetyl-L-isoleucine ethyl ester(4819-22-1)

Safety Data

• Hazardous Substances Data: 4819-22-1(Hazardous Substances Data)

Usage

General Description

N-Acetyl-L-isoleucine ethyl ester is a chemical compound that is derived from the amino acid L-isoleucine. It is often used as a supplement in the sports nutrition industry for its supposed ability to improve muscle function and exercise performance. N-Acetyl-L-isoleucine ethyl ester is believed to enhance protein synthesis and reduce muscle fatigue, making it a popular ingredient in pre-workout supplements and muscle-building products. Some research also suggests that it may have potential benefits for cognitive function and brain health, although more studies are needed to confirm these effects. Overall, N-Acetyl-L-isoleucine ethyl ester is a compound that is primarily used in the fitness and wellness industry for its potential performance-enhancing and muscle-supporting properties.

Upstream product

• 64-17-5 ethanol 
• 5854-47-7 (2S,3S)-N-acetyl-2-amino-3-methylpentanoic acid 
• 2256-90-8 ethyl N-acetyl-isoleucinate 
• 921-74-4 L-isoleucine ethyl ester 
• 75-36-5 acetyl chloride 

Downstream Products

• 3077-46-1 N-acetyl-L-isoleucine 
• 3077-46-1 N-acetyl-d-isoleucine 
• 2256-90-8 (R)-2-Acetylamino-3-methyl-pentanoic acid ethyl ester 

Relevant articles and documents

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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.