10491-09-5

Usage

Uses

Used in Pharmaceutical Industry:
H-D-ALA-D-ALA-D-ALA-D-ALA-D-ALA-OH is used as a target for antibiotics, specifically for vancomycin, which binds to the peptide and prevents its incorporation into the bacterial cell wall. This interaction leads to the disruption of bacterial cell wall synthesis and ultimately results in bacterial cell death, making it a crucial component in the development of antibiotics against certain bacteria.
Used in Peptide-based Drug Production:
H-D-ALA-D-ALA-D-ALA-D-ALA-D-ALA-OH is utilized as a component in the production of peptide-based drugs. Its specific sequence of amino acids allows for the development of drugs that can target and interact with specific biological systems, offering potential therapeutic benefits in various medical applications.
Used in Synthesis of Bioactive Compounds:
H-D-ALA-D-ALA-D-ALA-D-ALA-D-ALA-OH is employed as a component in the synthesis of various bioactive compounds. Its unique structure and properties make it a valuable building block for creating new compounds with potential applications in medicine, agriculture, and other industries.

Upstream product

• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 5874-90-8 L-ala-L-ala-L-ala 
• 926-78-3 tetra-L-alanine 
• 338-69-2 D-Alanine 

Downstream Products

• 10251-27-1 hexaalanine 

Relevant academic research and scientific papers

Mechanism study on the oligomerization of amino acids into peptides by phosphorus trichloride

As treated by phosphorus trichloride, amino acids could oligomerize into polypeptides. Based on the results obtained by 31P-NMR and ESI-MS/MS, a possible reaction mechanism was proposed. The mechanism might undergo a penta-coordinated phosphorus intermediat. The activated amino acid was a five-membered cyclic penta-coordinated phosphorus intermediate. The nucleophilic attack of the amino group from an amino acid or peptide on the carbonyl group of intermediate led to the formation of peptide and released one equivalent dichloride phosphoric acid. The repetition of the reaction sequence generated a series of oligopeptides. Copyright Taylor & Francis Group, LLC.

Structure and dynamics of the homologous series of alanine peptides: A joint molecular dynamics/NMR study

The φ,ψ backbone angle distribution of small homopolymeric model peptides is investigated by a joint molecular dynamics (MD) simulation and heteronuclear NMR study. Combining the accuracy of the measured scalar coupling constants and the atomistic detail of the all-atom MD simulations with explicit solvent, the thermal populations of the peptide conformational states are determined with an uncertainty of R helical conformations. No significant change in the distribution of conformers is observed with increasing chain length (Ala3 to Ala7). Trivaline samples all three major conformations significantly. Tryglycine samples the four corner regions of the Ramachandran space and exists in a slow conformational equilibrium between the cis and trans conformation of peptide bonds. The backbone angle distribution was also studied for the segment Ala3 surrounded by either three or eight amino acids on both N- and C-termini from a sequence derived from the protein hen egg white lysozyme. While the conformational distribution of the central three alanine residues in the 9mer is similar to that for the small peptides Ala3-Ala7, major differences are found for the 19mer, which significantly (30-40%) samples αR helical stuctures.