688-12-0

Basic information

• Product Name: CHLOROACETYL-L-LEUCINE
• Synonyms: n-chloroacetyl-l-leucinecrystalline;N-CHLOROACETYL-L-LEU;N-CHLOROACETYL-L-LEUCINE;CLAC-LEU-OH;CHLOROACETYL-L-LEUCINE;CHLOROAC-LEU-OH;N-(2-Chloroacetyl)-L-leucine;(S)-2-[(Chloroacetyl)amino]-4-methylpentanoic acid
• CAS NO: 688-12-0
• Molecular Formula: C₈H₁₄ClNO₃
• Molecular Weight: 207.65
• EINECS: 211-700-2
• Mol File: 688-12-0.mol
• Article Data: 3

Chemical Properties

• Melting Point: 134 °C
• Boiling Point: 401.1ºC at 760 mmHg
• Flash Point: 196.4ºC
• Appearance: /
• Density: 1.198g/cm3
• Vapor Pressure: 1.48E-07mmHg at 25°C
• Refractive Index: -15.5 ° (C=2, EtOH)
• Storage Temp.: Store at 0°C
• Solubility: almost transparency in Methanol
• PKA: 3.24±0.10(Predicted)
• CAS DataBase Reference: CHLOROACETYL-L-LEUCINE(CAS DataBase Reference)
• NIST Chemistry Reference: CHLOROACETYL-L-LEUCINE(688-12-0)
• EPA Substance Registry System: CHLOROACETYL-L-LEUCINE(688-12-0)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 688-12-0(Hazardous Substances Data)

Usage

General Description

CHLOROACETYL-L-LEUCINE is a chemical compound that belongs to the family of amino acids. It is a derivative of leucine, which is an essential amino acid that is important for protein synthesis and muscle growth. CHLOROACETYL-L-LEUCINE is often used in the field of biochemistry and pharmaceutical research as a building block for the synthesis of peptides and other complex molecules. Due to its specific chemical structure, it has the potential to be used in the development of drugs and medical treatments. CHLOROACETYL-L-LEUCINE is also used in the study of protein-protein interactions and molecular biology.

InChI:InChI=1/C8H14ClNO3/c1-5(2)3-6(8(12)13)10-7(11)4-9/h5-6H,3-4H2,1-2H3,(H,10,11)(H,12,13)/t6-/m1/s1

Upstream product

• 61-90-5 L-leucine 
• 79-04-9 chloroacetyl chloride 
• 869-19-2 Glycyl-L-leucine 
• 3886-69-9 (R)-1-phenyl-ethyl-amine 
• 27243-15-8 N-succinimidyl 2-chloroacetate 

Downstream Products

• 1389330-74-8 C₁₅H₂₁ClN₂O₂ 
• 1389330-73-7 C₁₄H₁₉ClN₂O₂ 
• 1389330-55-5 C₃₂H₄₉ClN₄O₆Si 
• 1389330-54-4 C₃₃H₅₂N₄O₆Si 
• 1389330-53-3 C₃₂H₅₀N₄O₆Si 
• 1389330-30-6 C₄₂H₅₀ClN₅O₄ 
• 1389330-29-3 C₄₃H₅₃N₅O₄ 
• 1389330-28-2 C₄₂H₅₁N₅O₄ 
• 1389330-27-1 C₂₂H₂₈ClN₃O₂ 
• 1389330-26-0 C₂₃H₃₁N₃O₂ 
• 1389330-25-9 C₂₂H₂₉N₃O₂ 
• 1389330-75-9 C₁₄H₁₈Cl₂N₂O₂ 
• 1417521-29-9 (S)-S-phenyl 2-(2-azidoacetamido)-4-methylpentanethioate 
• 40297-96-9 H-Gly-Leu-Met-NH₂ hydrochloride 

Relevant articles and documents

Investigation of peptoid chiral stationary phases terminated with N′-substituted phenyl-L-proline/leucine amide

Eight peptoid chiral stationary phases (CSPs) terminated with N′-substituted phenyl-L-proline or L-leucine amide were prepared and evaluated under normal phase mode. With 59 racemic analytes, we compared the enantiomeric separations on CSPs terminated with p-methylphenyl, p-chlorophenyl and unsubstituted phenyl. For short peptoid selectors containing only one S-N-(1-phenylethyl) glycine (Nspe) unit, the terminal p-methyl substituent did not affect chiral recognition abilities significantly. In L-proline amide terminated CSPs, p-chloro substituent resulted in obviously inferior selectivity while in L-leucine amide terminated CSPs, it worked much better. Longer peptoid selectors containing two more Nspe units generally performed much better than the shorter ones, due to the great contributions of peptoid chain to chiral recognition. Meanwhile, the effects of the terminal substituent on selectivity were found changed on these CSPs. For CSPs terminated with L-leucine amide, the terminal p-chloro substituent in longer selector no longer produced the best recognition ability; the CSP with unsubstituted phenyl instead performed best. Comparison of these peptoid CSPs varied in terminal substituents and chain length was conducted to gain a better understanding of the chiral recognition mechanism of this type CSP and promote the development of more useful CSPs. Copyright

Synthesis and transport studies of model dipeptides with modified N-terminal amino groups into E. coli K12 mutant strains

The synthesis of Interminable guanidine derivatives of three dipeptides Ala-Ala, Ala-Leu, Ala-Phe and three dipeptides containing betaine as an N-terminal amino acid: Bet-Ala, Bet-Leu, Bet-He has been carried out. The transport studies of the obtained pseudopeptides and corresponding natural peptides into E. coli Kl2 mutant strains have also been performed. The results indicate that modified dipeptides containing N-terminal guanidine or betaine are not transported into E. coli K12 cells.