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| Description | GHGVYGHGVYGHGPYGHGPYGHLYW (CAS: 2231617-62-0) is a 25-amino acid histidine-rich biomimetic mineralization peptide, containing 5 histidines (His, H), 9 glycines (Gly, G), 5 tyrosines (Tyr, Y), 2 valines (Val, V), 2 prolines (Pro, P), 1 leucine (Leu, L), and 1 tryptophan (Trp, W). The sequence design features: (1) rich histidine residues (5 His, 20%), whose imidazole groups (pKa ~6.0) have strong metal ion chelating ability, can coordinate with divalent metal ions such as Zn²⁺, Cu²⁺, Ni²⁺, and Ca²⁺, and serve as nucleation sites for biomimetic mineralization, inducing deposition and crystallization of inorganic minerals such as hydroxyapatite, calcium carbonate, and zinc oxide; (2) rich glycine residues (9 Gly, 36%), whose side chains are only hydrogen atoms, providing high conformational flexibility that allows the peptide chain to adapt to the geometry of mineral surfaces; glycine-rich sequences are also characteristic motifs of structural proteins such as collagen and silk fibroin; (3) multiple tyrosine residues (5 Tyr), whose phenolic hydroxyl groups can participate in metal ion coordination and oxidative crosslinking (e.g., tyrosinase-catalyzed or horseradish peroxidase-catalyzed dityrosine crosslinking), while the aromatic rings of tyrosine can participate in π-π stacking interactions to promote peptide self-assembly; (4) proline residues (2 Pro) that can introduce turns in the peptide chain, regulating peptide secondary structure and self-assembly behavior; (5) the C-terminal tryptophan residue providing intrinsic fluorescence for monitoring peptide conformational changes and self-assembly processes. This peptide can be used for: (1) biomimetic mineralization and bone/dental tissue engineering research as a mineralization template and hydroxyapatite nucleation site; (2) metal ion chelation and heavy metal adsorption materials; (3) construction of peptide self-assembling hydrogels and nanostructures; (4) biomineralization mechanism research; (5) mussel adhesive protein mimetic peptides and underwater adhesive research. GHGVYGHGVYGHGPYGHGPYGHLYW is an important tool for studying biomimetic mineralization and peptide-based biomaterials. |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| GHGVYGHGVYGHGPYGHGPYGHGLYW | Histidine/tyrosine-rich peptide; pH-responsive self-assembling peptide | pH-responsive self-assembly, histidine-rich peptide, biomaterial hydrogel, supramolecular assembly | Repeated sequence peptide rich in histidine, tyrosine and glycine; histidine imidazole groups have pH responsiveness, and self-assemble into nano-aggregates via hydrogen bonding and hydrophobic interactions at neutral pH | C₁₃₂H₁₆₃N₃₉O₃₃ | 2886.22 | ~2887.9 | Acetate | 23 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-GHG023 | White powder | Store at -20°C, sealed, dry and protected from light. Aliquot for storage. | Stable for 1 month at 2–8°C in sealed dry condition; stable for shipping at ambient temperature. | Stable for 7 days at 4°C. Soluble in dilute acetic acid and acidic buffers. Histidine-rich sequence with pH responsiveness; protonated imidazole groups confer excellent solubility under acidic conditions; prone to hydrophobic self-assembly and aggregation at neutral pH. | Stable for 2 years at -20°C, dry and protected from light. |
Functional Description
| Product Code | Frontend Short Summary (for search list display) | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-GHG023 | Histidine/tyrosine-rich self-assembling peptide as pH-responsive supramolecular biomaterial | This histidine-rich peptide is a pH-responsive self-assembling biomaterial. Under acidic conditions, histidine imidazole groups protonate and the peptide remains soluble and dispersed. At neutral pH, deprotonated imidazoles drive peptide self-assembly via hydrogen bonding, π-π stacking and hydrophobic interactions, forming nanofibers, hydrogels and other supramolecular structures for smart responsive hydrogels and controlled release carriers. | Biomaterials & hydrogels, smart drug delivery, supramolecular self-assembly, tissue engineering scaffolds, pH-responsive materials | Histidine imidazole hydrogen bonding site; tyrosine π-π stacking; hydrophobic interaction assembly |
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