H-Gly-Hyp-Ala-OH contains hydroxyproline, which introduces hydrogen-bonding versatility and mimics collagen-like environments. Glycine enhances flexibility while alanine supports simple secondary-structure motifs. Researchers analyze its conformational behavior in hydration studies. Applications include collagen-mimetic research, SPPS calibration, and structural-probe development.
CAT No: R2606
CAS No:62147-09-5
Synonyms/Alias:H-GLY-HYP-ALA-OH;62147-09-5;(S)-2-((2S,4R)-1-(2-Aminoacetyl)-4-hydroxypyrrolidine-2-carboxamido)Propanoic acid;
H-Gly-hyp-ala-OH is a synthetic tripeptide composed of glycine, hydroxyproline, and alanine, designed to model structural motifs commonly found in collagen and related extracellular matrix proteins. As a peptide compound, it holds significant value in biochemical research, particularly in studies investigating peptide structure-function relationships, protein engineering, and extracellular matrix biology. Its unique sequence, featuring hydroxyproline—a post-translationally modified amino acid critical to collagen stability—makes it a versatile tool for exploring peptide folding, intermolecular interactions, and the physicochemical properties that govern protein architecture. The tripeptide's defined structure and compositional relevance to natural systems position it as an important reagent for both fundamental research and applied studies in biomaterials science.
Structural biology research: In the field of structural biology, H-Gly-hyp-ala-OH serves as a model peptide for elucidating the role of hydroxyproline in stabilizing the collagen triple helix. By incorporating this tripeptide into biophysical assays such as circular dichroism spectroscopy or nuclear magnetic resonance, researchers can dissect the contributions of each residue—particularly hydroxyproline—to secondary structure formation, hydrogen bonding patterns, and overall peptide conformation. These insights support the rational design of collagen-mimetic materials and inform our understanding of protein folding diseases related to extracellular matrix dysfunction.
Peptide synthesis and method development: The sequence provides a valuable standard for optimizing peptide synthesis protocols, especially when incorporating challenging residues like hydroxyproline. Synthetic chemists and method developers utilize H-Gly-hyp-ala-OH to benchmark coupling efficiencies, test new protecting group strategies, and refine purification methods for proline-rich peptides. Its well-characterized structure enables reliable assessment of synthetic yields and product integrity, facilitating advances in solid-phase peptide synthesis and post-synthetic modification techniques.
Biomaterials and tissue engineering: The tripeptide's resemblance to collagen motifs makes it an attractive building block for designing biomimetic scaffolds and hydrogels. Researchers in tissue engineering employ this compound to investigate cell-adhesion properties, matrix remodeling, and the impact of specific peptide sequences on cellular behavior. By integrating H-Gly-hyp-ala-OH into synthetic matrices, it becomes possible to systematically explore how sequence variations influence mechanical strength, degradation rates, and bioactivity—critical parameters for developing advanced regenerative materials.
Enzymology and protease specificity studies: H-Gly-hyp-ala-OH is frequently used as a substrate in enzymatic assays designed to probe the specificity and catalytic activity of proteases, particularly those that recognize proline- and hydroxyproline-containing sequences. Its defined length and composition allow for precise measurement of enzyme kinetics, substrate binding affinities, and cleavage site preferences. These studies contribute to the characterization of matrix metalloproteinases, prolyl hydroxylases, and other enzymes relevant to extracellular matrix turnover and remodeling.
Analytical method calibration: The tripeptide also functions as a reference standard in analytical chemistry, supporting the development and validation of chromatographic and mass spectrometric methods. Laboratories use it to calibrate retention times, optimize ionization conditions, and evaluate the sensitivity and selectivity of detection systems for small peptides. Its consistent behavior under analytical conditions ensures accurate quantification and identification in complex biological samples, thereby enhancing the reliability of peptide-based assays and workflows.
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