Asn-Gly-Leu-Pro-Gly-Pro-Ile-Gly-Hyp emulates collagen-like motifs through interspersed glycine, proline, and hydroxyproline residues. Researchers investigate its triple-helix formation tendencies and hydration behavior. The sequence aids modeling of extracellular-matrix assembly. Applications include biomaterial development, peptide-folding analysis, and collagen-mimetic research.
CAT No: R2602
CAS No:620583-64-4
Synonyms/Alias:EX-A9237;Asn-Gly-Leu-Pro-Gly-Pro-Ile-Gly-Hyp;620583-64-4;
Asn-Gly-Leu-Pro-Gly-Pro-Ile-Gly-Hyp is a synthetic peptide composed of a specific sequence of amino acids, including hydroxyproline at the C-terminus. As a custom-designed oligopeptide, it serves as a valuable tool in the investigation of protein structure-function relationships, molecular recognition events, and the biophysical properties of peptide chains. Its defined composition and sequence make it particularly relevant for studies focused on collagen-like motifs and the role of post-translational modifications such as hydroxylation in peptide stability and biological interactions. The incorporation of hydroxyproline, a hallmark of collagen and related extracellular matrix proteins, further enhances its significance in both fundamental and applied biochemical research.
Peptide structure-function analysis: Researchers utilize this peptide in the detailed examination of how specific amino acid arrangements, especially those featuring hydroxyproline, influence the conformational dynamics and stability of peptide chains. By synthesizing and studying such sequences, scientists can dissect the contributions of individual residues to overall peptide folding, secondary structure formation, and resistance to enzymatic degradation. Insights gained from these studies inform broader understanding of protein folding disorders, peptide design principles, and the development of biomimetic materials.
Collagen-mimetic studies: The presence of hydroxyproline in the peptide sequence renders it a pertinent model for investigating the biophysical and biochemical properties of collagen and collagen-like proteins. It serves as a substrate in assays designed to probe triple-helix formation, intermolecular interactions, and the impact of post-translational modifications on extracellular matrix assembly. These applications are crucial for advancing knowledge in tissue engineering, regenerative medicine research, and the design of novel biomaterials that emulate the mechanical and structural attributes of native collagen.
Enzymatic substrate assays: The defined sequence of this peptide makes it an effective substrate for characterizing the activity of proteases, peptidases, and other enzymes involved in extracellular matrix remodeling. By monitoring the enzymatic cleavage patterns and kinetics, researchers can elucidate enzyme specificity, substrate preferences, and the influence of sequence modifications on proteolytic susceptibility. Such assays are instrumental in drug discovery, enzyme engineering, and the validation of biochemical pathways implicated in tissue development and disease.
Biophysical characterization: The peptide is frequently employed in spectroscopic and calorimetric analyses aimed at quantifying parameters such as thermal stability, hydrogen bonding, and molecular interactions. Techniques including circular dichroism, nuclear magnetic resonance, and differential scanning calorimetry benefit from the use of well-defined peptides like this one to benchmark experimental conditions and interpret the effects of sequence variation. These studies enhance our understanding of peptide energetics and inform the rational design of stable, functional peptide-based materials.
Peptide synthesis optimization: In the context of synthetic chemistry, this peptide sequence serves as a model for refining solid-phase peptide synthesis protocols, particularly those involving non-standard amino acids like hydroxyproline. Its assembly challenges and post-synthetic handling provide valuable feedback on coupling efficiencies, protecting group strategies, and purification workflows. Optimization efforts guided by such model peptides contribute to the development of more robust and scalable synthetic methodologies for complex peptide products.
3. Implications of ligand-receptor binding kinetics on GLP-1R signalling
5. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More