Hexapeptide-12 (Val-Gly-Val-Ala-Pro-Gly) contains alternating hydrophobic, flexible, and turn-inducing residues, favoring β-turn and extended-coil structures. The motif is frequently explored in dermal-matrix and extracellular-matrix interaction studies. Researchers evaluate its impact on collagen-related signaling and peptide-matrix adhesion. Applications include cosmetic-peptide research, biomaterial functionalization, and structural-motif analysis.
CAT No: R2589
CAS No:92899-39-3
Synonyms/Alias:92899-39-3;Chemotactic Domain of Elastin;Val-Gly-Val-Ala-Pro-Gly;H-Val-Gly-Val-Ala-Pro-Gly-OH;04V1QPJ5TW;2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-amino-3-methylbutanoyl]amino]acetyl]amino]-3-methylbutanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]acetic acid;Vgvapg;hexapeptide-12 (val-gly-val-ala-pro-gly);2-((S)-1-((S)-2-((S)-2-(2-((S)-2-Amino-3-methylbutanamido)acetamido)-3-methylbutanamido)Propanoyl)pyrrolidine-2-carboxamido)acetic acid;Val-gly-ala-pro-gly;UNII-04V1QPJ5TW;Valyl-glycyl-valyl-alanyl-prolyl-glycine;L-Glycine High;MFCD00133914;DERMAXYL;L-Glycine7407;L-Glycine High7408;SCHEMBL1404295;DTXSID50918909;HY-P4998;FC108662;CS-0675630;H-Val-Gly-Val-Ala-Pro-Gly-OH; H-VGVAPG-OH;Glycine, L-valylglycyl-L-valyl-L-alanyl-L-prolyl-;Q27247699;Chemotactic Domain of Elastin (H-L-Val-Gly-L-Val-L-Ala-L-Pro-Gly-OH);Glycine, N-(1-(N-(N-(N-L-valylglycyl)-L-valyl)-L-alanyl)-L-prolyl)-, (SP-4-2)-;N-[(1-{N-[2-({2-[(2-Amino-1-hydroxy-3-methylbutylidene)amino]-1-hydroxyethylidene}amino)-1-hydroxy-3-methylbutylidene]alanyl}pyrrolidin-2-yl)(hydroxy)methylidene]glycine;
Hexapeptide-12 (val-gly-val-ala-pro-gly) is a synthetic peptide composed of six amino acids arranged in a specific sequence, designed to mimic or modulate naturally occurring peptide interactions in biological systems. As a member of the oligopeptide family, it exhibits distinct physicochemical properties that make it valuable for a range of biochemical and molecular research applications. Its defined structure and sequence-specific behavior allow researchers to explore peptide-mediated signaling pathways, protein-protein interactions, and the functional consequences of sequence motifs within biological contexts. The versatility and stability of Hexapeptide-12 render it a useful tool for investigating the roles of short peptides in cellular communication and structural assembly.
Peptide signaling studies: Hexapeptide-12 is frequently employed in research focused on elucidating the mechanisms of peptide-mediated cell signaling. Its sequence, which features a combination of hydrophobic and flexible residues, enables it to serve as a model substrate or ligand in assays examining receptor binding, intracellular signaling cascades, or the modulation of cellular responses. By providing a reproducible system for probing how short peptides interact with membrane-bound or soluble receptors, it contributes to a deeper understanding of communication pathways that regulate cell behavior.
Protein-protein interaction assays: The defined structure of this hexapeptide makes it an effective probe for studying the specificity and affinity of protein-protein interactions. Researchers utilize it in techniques such as surface plasmon resonance, pull-down assays, and co-immunoprecipitation to characterize binding motifs and interaction domains within larger protein complexes. Its application in these studies supports the identification of critical contact points and the mapping of interaction networks essential for cellular function.
Peptide synthesis benchmarking: As a representative oligopeptide, Hexapeptide-12 serves as a standard in the optimization and validation of solid-phase peptide synthesis protocols. Its moderate length and well-characterized sequence allow synthetic chemists to evaluate coupling efficiencies, resin compatibility, and purification strategies. By benchmarking synthesis and analytical workflows with this peptide, laboratories can refine methodologies, ensuring reproducibility and high-quality outputs for more complex peptide projects.
Structure-activity relationship (SAR) research: The modular nature of Hexapeptide-12 enables its use in SAR studies aimed at deciphering the contributions of individual amino acid residues to overall biological activity. By systematically substituting or modifying residues within the sequence, researchers can assess the impact on binding, stability, or functional performance in various bioassays. These investigations facilitate the rational design of peptide analogs with enhanced or tailored properties for downstream applications.
Biomaterials and surface functionalization: Owing to its sequence-defined architecture, Hexapeptide-12 is utilized in the development of peptide-functionalized biomaterials. It can be immobilized onto surfaces or integrated into polymer matrices to confer specific biological recognition or interaction capabilities. Such functionalized materials are valuable in biosensor development, tissue engineering scaffolds, and other applications where precise control over cell-material interactions is required. By leveraging the unique properties of this hexapeptide, researchers can create advanced materials with tunable bioactivity and selectivity.
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