H-Gly-Ala-Hyp-OH integrates hydroxyproline with flexible glycine and helix-supporting alanine to study backbone curvature. Researchers investigate its hydrogen-bonding patterns and solvent interactions. The tripeptide aids exploration of collagen-like motifs. Applications include peptide-material modeling, secondary-structure analysis, and synthetic design.
CAT No: R2353
CAS No:22028-81-5
Synonyms/Alias:H-Gly-Ala-Hyp-OH;22028-81-5;(2S,4R)-1-[(2S)-2-[(2-aminoacetyl)amino]propanoyl]-4-hydroxypyrrolidine-2-carboxylic acid;(2S,4R)-1-((S)-2-(2-Aminoacetamido)Propanoyl)-4-hydroxypyrrolidine-2-carboxylic acid;MFCD00237895;HY-P4231;DA-64145;FG108945;CS-0653246;
H-Gly-Ala-Hyp-OH is a synthetic tripeptide composed of glycine, alanine, and hydroxyproline residues, designed to mimic sequences commonly found in collagen and related extracellular matrix proteins. As a peptide compound, it holds significant relevance in biochemical research focused on protein structure, peptide interaction dynamics, and extracellular matrix biology. The presence of hydroxyproline, a post-translationally modified amino acid, further enhances its utility in studies investigating collagen stability and the molecular mechanisms underlying connective tissue function. Researchers utilize this tripeptide to probe structural motifs, model peptide folding, and explore enzymatic processes relevant to peptide modification and degradation.
Peptide structure-function analysis: In peptide and protein biochemistry, H-Gly-Ala-Hyp-OH serves as a valuable model for elucidating the structural roles of hydroxyproline in polypeptide chains. The sequence offers a simplified system to dissect how hydroxyproline incorporation influences backbone conformation, hydrogen bonding, and secondary structure formation, particularly in the context of collagen-like peptides. Experimental studies employing this tripeptide can yield insights into the stabilization mechanisms imparted by hydroxyproline, supporting the rational design of biomimetic materials and engineered proteins.
Collagen biomimicry research: The tripeptide is frequently employed in investigations aiming to replicate or understand the unique triple-helical architecture of collagen. Its sequence, incorporating both alanine and hydroxyproline, enables researchers to model critical aspects of collagen's repeating motifs, facilitating the study of peptide self-assembly, thermal stability, and molecular recognition events. Such research is instrumental in the development of synthetic scaffolds for tissue engineering and in the creation of novel biomaterials inspired by natural extracellular matrices.
Enzymatic substrate studies: H-Gly-Ala-Hyp-OH functions as a defined substrate in enzymology experiments focused on collagen-modifying or collagen-degrading enzymes, such as prolyl hydroxylases and matrix metalloproteinases. By providing a controlled peptide substrate, it allows for detailed kinetic and mechanistic analyses of enzyme specificity, catalytic efficiency, and post-translational modification processes. These studies contribute to a deeper understanding of extracellular matrix remodeling and the regulation of connective tissue homeostasis at the molecular level.
Analytical method development: The tripeptide's well-defined composition and sequence make it an excellent standard or reference material in analytical biochemistry. It is utilized in method validation for chromatographic separation, mass spectrometric detection, and peptide quantification protocols. Scientists leverage its predictable physicochemical properties to calibrate instruments, assess method sensitivity, and optimize sample preparation techniques for peptide-based analyses.
Peptide synthesis optimization: H-Gly-Ala-Hyp-OH is also applied in the evaluation and refinement of solid-phase peptide synthesis (SPPS) strategies, particularly for sequences containing hydroxyproline. Its use enables researchers to assess coupling efficiencies, deprotection conditions, and overall synthetic yields when incorporating modified amino acids. Such optimization is essential for advancing peptide manufacturing technologies and ensuring the reliable production of structurally complex or functionally specialized peptides for research and industrial applications.
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