H-Ala-β-Ala-OH combines standard alanine with β-alanine to study backbone extension and flexibility. The sequence enables analysis of noncanonical residue incorporation into peptide frameworks. Researchers examine its solubility, hydrogen bonding, and structural transitions. Applications include synthetic method development, polymer-peptide modeling, and conformational research.
CAT No: R2670
CAS No:52788-02-0
Synonyms/Alias:H-Ala-Beta-Ala-OH;52788-02-0;CHEMBL189696;3-[[(2S)-2-aminopropanoyl]amino]propanoic acid;L-Alanine-|A-alanine;L-Alanyl-.beta.-alanine;SCHEMBL7290633;LHMWTJPMNYKPGC-BYPYZUCNSA-N;BDBM50169124;(S)-3-(2-aminopropanamido)propanoic acid;3-((S)-2-Amino-propionylamino)-propionic acid;
H-Ala-Beta-Ala-OH is a synthetic dipeptide consisting of an N-terminal L-alanine residue linked via a peptide bond to β-alanine, terminating in a free carboxylic acid group. As a member of the peptide compound family, this molecule features both a standard α-amino acid (L-alanine) and a non-proteinogenic β-amino acid (β-alanine), providing a unique structural motif for biochemical investigations. Its hybrid composition offers valuable opportunities for studying peptide backbone modifications, conformational effects, and structure-activity relationships. The distinct properties of H-Ala-Beta-Ala-OH make it a versatile tool in peptide research, enabling the exploration of novel peptide architectures and functional behaviors relevant to enzymology, biophysics, and chemical biology.
Peptide synthesis research: H-Ala-Beta-Ala-OH serves as a useful building block for solid-phase and solution-phase peptide synthesis, particularly in the construction of peptides containing β-amino acid residues. Incorporation of β-alanine into peptide chains is of significant interest due to its ability to disrupt regular secondary structures, such as α-helices and β-sheets, thereby enabling the design of peptides with altered folding patterns and enhanced resistance to enzymatic degradation. Researchers utilize this dipeptide to investigate how β-residues influence overall peptide stability, backbone flexibility, and bioactive conformations.
Structure-activity relationship studies: The inclusion of a β-amino acid within a dipeptide framework allows for the systematic evaluation of how backbone modifications affect biological recognition and molecular interactions. By comparing analogs containing H-Ala-Beta-Ala-OH to those with only α-amino acids, scientists can assess the impact of β-alanine on binding affinity, selectivity, and functional outcomes in target assays. These studies are essential for advancing the rational design of peptidomimetics and optimizing lead compounds for biochemical applications.
Protease substrate and inhibitor design: The unique backbone configuration of H-Ala-Beta-Ala-OH makes it a valuable component in the development of protease substrates and inhibitors. β-Amino acid residues are known to confer resistance to proteolytic cleavage, which can be exploited to create model peptides for studying enzyme specificity or engineering stable peptide-based inhibitors. The dipeptide can be integrated into substrate libraries or inhibitor scaffolds to probe the substrate tolerance and active site preferences of various proteolytic enzymes.
Biophysical and conformational analysis: As a model system, H-Ala-Beta-Ala-OH is frequently employed in spectroscopic and computational studies aimed at elucidating the conformational dynamics of peptides containing β-amino acids. Its defined sequence enables detailed examination of backbone torsion angles, hydrogen bonding patterns, and solvent interactions. Such investigations provide fundamental insights into the physicochemical principles governing peptide folding and stability, informing the design of novel foldamers and bioinspired materials.
Analytical method development: The distinct chemical and structural features of H-Ala-Beta-Ala-OH render it a practical reference standard for developing and validating analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its well-characterized behavior under various analytical conditions assists researchers in calibrating instruments, optimizing separation protocols, and establishing detection parameters for peptides containing non-standard amino acid residues. These capabilities support quality control and method optimization in peptide chemistry laboratories.
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