(Prolyl-hydroxylprolyl-glycine)10 is a repetitive triplet peptide mimicking collagen-like motifs with hydroxylated proline contributing to stability. The sequence supports research on triple-helix formation, fibril organization, and peptide-mineral interactions. Researchers use it to model collagen assembly and biomechanical properties. Its repeating architecture promotes structured supramolecular organization.
CAT No: R1899
CAS No:40350-90-1
Synonyms/Alias:(Prolyl-hydroxylprolyl-glycine)10;(Pro-hyp-gly)10;40350-90-1;Glycine, L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolylglycyl-L-prolyl-4-hydroxy-L-prolyl-;
Chemical Name:2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-[(2S)-1-[2-[[(2S,4R)-4-hydroxy-1-(pyrrolidine-2-carbonyl)pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetic acid
Prolyl-hydroxylprolyl-glycine)10 is a synthetic peptide composed of repeating tripeptide units, specifically proline, hydroxyproline, and glycine. As a biomimetic sequence, it reflects the characteristic motif found in collagen, one of the most abundant structural proteins in mammals. This repetitive arrangement is critical for the formation of the collagen triple helix, lending the peptide significant value in research focused on extracellular matrix biology, protein engineering, and biomaterials development. The unique sequence and structure of (Prolyl-hydroxylprolyl-glycine)10 make it a versatile tool for investigating the physicochemical properties and biological functions associated with collagen-like peptides.
Peptide synthesis research: In peptide chemistry, (Prolyl-hydroxylprolyl-glycine)10 serves as an essential model for studying the solid-phase synthesis and folding of collagen-mimetic peptides. Its defined sequence allows researchers to evaluate coupling efficiencies, optimize reaction conditions, and analyze sequence-specific modifications. The presence of hydroxyproline is particularly relevant for assessing post-synthetic modifications and their impact on peptide stability, conformation, and solubility, thereby advancing the understanding of synthetic strategies for complex peptides.
Structural biology studies: The tripeptide repeat within this compound provides a robust platform for elucidating the mechanisms underlying collagen triple helix formation and stability. Researchers utilize (Prolyl-hydroxylprolyl-glycine)10 to investigate hydrogen bonding patterns, helix propagation, and the influence of hydroxyproline on thermal stability. These insights are vital for deciphering how sequence and post-translational modifications dictate the mechanical and thermal properties of collagen and related biomaterials.
Biomaterials development: Owing to its collagen-mimetic nature, the peptide is widely employed in the design and fabrication of advanced biomaterials. Scientists incorporate (Prolyl-hydroxylprolyl-glycine)10 into hydrogels, scaffolds, and coatings to mimic the structural and functional attributes of natural extracellular matrices. Such applications are instrumental in tissue engineering, regenerative medicine research, and the development of cell culture substrates that promote specific cellular responses, such as adhesion, proliferation, and differentiation.
Protein-protein interaction assays: The defined sequence and structure of this peptide make it an ideal probe for studying interactions between collagen and its binding partners, including integrins, matrix metalloproteinases, and other extracellular matrix components. By serving as a substrate or ligand in binding assays, (Prolyl-hydroxylprolyl-glycine)10 enables detailed analysis of recognition motifs, affinity parameters, and the molecular basis of matrix assembly and remodeling.
Analytical method development: The peptide's well-characterized composition and predictable behavior in analytical techniques such as mass spectrometry, circular dichroism, and chromatography provide a reliable standard for method validation. Researchers leverage (Prolyl-hydroxylprolyl-glycine)10 to calibrate instruments, optimize detection protocols, and benchmark the performance of analytical workflows targeting collagen-like sequences. This utility supports reproducibility and accuracy in both qualitative and quantitative peptide analysis across various research settings.
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