19245-87-5

Usage

Uses

Used in Pharmaceutical Industry:
AC-ALA-ALA-OH is used as a drug delivery agent for its ability to enhance the solubility and bioavailability of therapeutic agents. Its unique structure allows for better penetration and absorption, improving the overall efficacy of the drug.
Used in Wound Healing Applications:
AC-ALA-ALA-OH is used as a wound healing agent due to its potential to promote tissue regeneration and repair. Its properties may contribute to faster healing and improved outcomes in various types of wounds.
Used in Anticancer Applications:
AC-ALA-ALA-OH is used as an anticancer agent for its potential to target and inhibit the growth of cancer cells. Its unique structure may allow for selective targeting of cancer cells, reducing side effects and improving treatment outcomes.

Upstream product

• 30802-26-7 N-acetyl-L-alanyl-L-alanine methyl ester 
• 1948-31-8 di-L-alanine 
• 108-24-7 acetic anhydride 
• 60654-47-9 Ac-L-AlaN₂H₃ 
• 2483-51-4 N-[(benzyloxy)carbonyl]-L-alanyl-L-alanine methyl ester 
• 41036-19-5 L-alanyl-alanine methylester hydrochloride 
• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 

Downstream Products

• 30802-29-0 Ac-Ala-Ala-Ala-Ala-OMe 
• 38320-48-8 Ac-Ala₂-AlaCH₂Cl 
• 90302-96-8 Ac-Ala₃-PheCH₂Cl 
• 90302-99-1 Ac-Ala₂-Pro-PheCH₂Cl 
• 90302-97-9 Ac-Ala₂-Leu-PheCH₂Cl 
• 90302-98-0 Ac-Ala₂-Phe-PheCH₂Cl 

Relevant academic research and scientific papers

Conjugation of Short Peptides to Dibenzodiazepinone-Type Muscarinic Acetylcholine Receptor Ligands Determines M2R Selectivity

Muscarinic acetylcholine receptors (MRs), comprising five subtypes (M1R-M5R) in humans, exhibit a high degree of structural similarity. Therefore, subtype-selective MR agonists and antagonists are lacking. We present an approach to highly M2R-selective MR antagonists based on the conjugation of di- or tripeptides to M2R-preferring dibenzodiazepinone-type MR antagonists. M2R selectivity was dependent on the peptide sequence and on the type of linker. The introduction of basic amino acids resulted in improved M2R selectivity (e.g., UR-AP148 (48): pKi (hM2R) of 8.97, ratio of Ki M1R/M2R/M3R/M4R/M5R of 49:1:6500:60:400) compared to reported pyridobenzo- and dibenzodiazepinone-type MR ligands. A supposed dualsteric binding mode of the DIBA-peptide conjugates, such as 48, at MRs was supported by molecular dynamics simulations.

Hydrogen Bonded Squaramide-Based Foldable Module Induces Both β- And α-Turns in Hairpin Structures of α-Peptides in Water

A novel tertiary squaramido-based reverse-turn module SQ is reported, and its conformational properties are evaluated. This module is easily incorporated into a α-peptide sequence by conventional solid-phase peptide synthesis. The structure characterizati

The dimethylsulfoxonium methylide as unique reagent for the simultaneous deprotection of amino and carboxyl function of N-Fmoc-α-amino acid and N-Fmoc-peptide esters

The dimethylsulfoxonium methylide is described as a unique and useful reagent for the simultaneous deprotection of amino and carboxyl function of N-Fmoc-α-amino acid and N-Fmoc-peptide esters. The new methodology was applied successfully both to solution- and solid-phase peptide synthesis. The adopted methodology was extended successfully also to peptides containing amino acids bearing acid-sensitive protecting group in side chains. Furthermore no measurable epimerization was observed in the deprotection reaction of N-Fmoc-dipeptide methyl esters with dimethylsulfoxonium methylide.

Synthesis and in vitro enzyme activity of peptide derivatives of bacterial cell wall biosynthesis inhibitors

The enzyme diaminopimelate aminotransferase (DAP-AT) is a good potential target for the design of novel antibacterial agents. We have synthesised a series of peptide hydrazines based on the structure of the natural substrate of DAP-AT. These compounds show varied inhibition properties in vitro vs. DAP-AT from E. coli as well as moderate antimicrobial activity vs. E. coli. Examination of the kinetics of inhibition reveals that hydrazine, as well as the substituted hydrazino-peptides, shows two-phase slow-binding inhibition. Possible mechanisms for inhibition are discussed. The Royal Society of Chemistry 2000.

Thermitase - A Thermostable Serine Protease. I. Synthesis of Alanine Peptide Esters as Substrates of the Enzyme

The synthesis of N-acetylated and N-succinylated peptide esters of alanine is described.The peptides are built up from the Z-protected peptides by liquid phase fragment condensation and by acylation of the deprotected peptide esters.The kinetic parameters Km and kcat of some compounds are presented.

Thermitase - A Thermostable Serine Protease. II. Synthesis of Substrate Analogous Peptide Chloromethyl Ketones as Irreversibly Acting Inhibitors

The preparation of dipeptide to pentapeptide chloromethyl ketones of alanine with variation of the amino acid in the P1 and P2 position of the peptides is described.The synthesis is performed by fragment condensation of N-acylated amino acids or peptides with the unprotected chloromethyl ketone derivatives of amino acids and peptides, respectively.Some examples of enzyme inactivation by peptide chloromethyl ketones are discussed.