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| Description | GAIIGLMVGGVV (residues 29–40), the C-terminal hydrophobic packing stretch; used to dissect C-terminal β-sheet packing and fibril elongation. |
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) |
| β-Amyloid (29-40), human (human amyloid-β residues 29–40, 12-mer, GAIIGLMVGGVV) | Aβ(29-40); Amyloid β-Protein (29-40); GAIIGLMVGGVV; CAS 184865-04-1 | β-amyloid peptide, Aβ(29-40), pure hydrophobic C-terminal segment, GAIIGLMVGGVV, transmembrane-like hydrophobic core, strong aggregation/fibrillation, membrane insertion/toxicity, Alzheimer's disease | Linear 12-mer; free N-terminal Gly and free C-terminal Val carboxylic acid (-COOH); sequence GAIIGLMVGGVV; a pure hydrophobic C-terminal transmembrane-like segment composed almost entirely of hydrophobic residues (G/A/I/L/M/V); contains the Met35 oxidation-sensitive site; is the core hydrophobic segment driving strong Aβ40/42 aggregation and membrane interactions | C49H88N12O13S | 1084.63 | 1085.4 | Free base; CAS 184865-04-1 | 12 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-BAβ29-40-01 | White powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~2 years. Extremely hydrophobic and aggregation-prone; HFIP pre-treatment and aliquoting recommended. | 2–8°C for up to ~1 week; working aliquots at −80°C. | Practically insoluble in water; strongly hydrophobic. Must be dissolved in DMSO, HFIP, or hexafluoroisopropanol: first prepare a 1–2 mM stock in pure DMSO/HFIP with sonication, then dilute into buffer to the working concentration (organic phase ≤10%); in solution keep at 4°C for ≤24 h or aliquot at −80°C. Met35 is oxidation-sensitive; avoid repeated oxidant exposure. | solid stable for ~2 years at −20°C, sealed and desiccated; hygroscopic and aggregation-prone, keep dry and protected from light. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-BAβ29-40-01 | Synthetic human Aβ(29-40) 12-mer, the pure hydrophobic C-terminal transmembrane-like segment GAIIGLMVGGVV; strongly aggregating and water-insoluble; used to study C-terminal-hydrophobic-core-driven fibrillation, membrane insertion/damage, and Met35 oxidation; white powder requiring DMSO/HFIP cosolvent. | The C-terminal residues 29–40 of amyloid-β (Aβ; GAIIGLMVGGVV) form a transmembrane-like hydrophobic helix composed almost entirely of hydrophobic residues (Gly, Ala, Ile, Leu, Met, Val), and is considered the key driving force for stable β-sheet fibril formation by Aβ40/42. Unlike the hydrophilic N-terminal metal-binding region and the central charged region, this segment is highly hydrophobic and water-insoluble yet spontaneously forms abundant β-sheet aggregates in vitro that stain with ThT. Its research value includes (1) serving alone as a short-peptide model to isolate the contribution of the C-terminal hydrophobic core to aggregation without interference from N-terminal/central charged residues; (2) studying Aβ insertion into membranes/liposomes, pore formation, and membrane-damaging toxicity, as this hydrophobic segment is the main mediator of membrane interactions; (3) Met35 is an oxidation-sensitive site whose oxidation (MetO) markedly alters Aβ hydrophobicity, aggregation, and neurotoxicity, making this segment the minimal model for Met35-oxidation regulation; (4) serving as a screening substrate for anti-aggregation drugs, especially inhibitors targeting the C-terminal hydrophobic cavity. Due to its strong hydrophobicity, this segment must be dissolved in DMSO/HFIP. CAS 184865-04-1. | Alzheimer's disease (AD), C-terminal-hydrophobic-core-driven fibrillation, membrane insertion/pore formation/membrane damage, Met35 oxidation (MetO) regulation, anti-aggregation drug screening (C-terminal hydrophobic cavity), short-peptide hydrophobic aggregation model | C-terminal hydrophobic core self-aggregation; membrane lipid-bilayer insertion; Met35 redox regulation; C-terminal hydrophobic-cavity drug-binding site |
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