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| Description | QKLVFFAED (residues 16–22) contains both the KLVFF self-recognition motif and Glu22 (Dutch E22Q/Arctic E22G/Italian E22K hotspot); a key model for core nucleation and E22 mutation effects. |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure (Sequence) | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Amyloid β-Protein (16-22), human (human amyloid-β residues 16–22, 7-mer; the minimal motif containing the central hydrophobic core LVFFA) | Aβ(16-22); β-Amyloid (16-22); KLVFFAE; central-hydrophobic-core model peptide | β-amyloid fragment, Aβ central hydrophobic core (CHC), LVFFA nucleation motif, β-sheet nucleation model, minimal self-aggregating peptide, aggregation-inhibitor target model, ThT fibrillation, Alzheimer's disease | Linear 7-mer: H-Lys-Leu-Val-Phe-Phe-Ala-Glu-OH (KLVFFAE), corresponding to human Aβ residues 16–22. It fully contains the Aβ central hydrophobic core (CHC) LVFFA (17–21) flanked by charged residues Lys16 and Glu22, and is the shortest, most widely studied model peptide for intermolecular β-pairing and fibril nucleation. After HFIP pre-treatment it spontaneously self-assembles in aqueous buffer into anti-parallel β-sheets, oligomers and fibrils and gives a positive ThT fluorescence curve. | C43H64N8O10 | 852.47 | 853.03 | TFA salt ; CAS 153247-41-7 | 7 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-AB1622-01 | White powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~2 years. Although short, the peptide contains the strongly hydrophobic LVFFA core and is hygroscopic and prone to slow aggregation in the solid state; keep dry, dark and sealed. | 2–8°C for ~1–2 weeks; equilibrate to room temperature before opening to avoid moisture uptake; ship on blue ice, or dry ice in summer to limit heat-induced aggregation. | Solubility is moderate to poor: despite being only 7 residues, the strong LVFFA hydrophobicity makes it poorly soluble in pure water. Pre-treat with a small amount of HFIP (1,1,1,3,3,3-hexafluoro-2-propanol) with sonication to de-aggregate/disperse, evaporate under nitrogen, then dissolve in DMSO or buffer (PBS, pH 7.4); if needed, use DMSO at 5–20% as co-solvent. Prepare working solutions fresh and keep on ice; keep in solution at 4°C for only a few days, or aliquot and store at −20°C; avoid repeated freeze-thaw to prevent premature aggregation. | solid stable for ~2 years at −20°C, sealed, desiccated, protected from light; hygroscopic-weigh and aliquot quickly in a desiccator; no Met/Cys so no oxidation concern, but keep dark and dry. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Receptors |
| PEP-AB1622-01 | Human Aβ(16-22) heptapeptide KLVFFAE that fully retains the central hydrophobic core LVFFA; it is the minimal model peptide for Aβ β-sheet nucleation and fibril formation. It spontaneously self-assembles into β-sheet oligomers/fibrils and is ThT-positive. Used to study nucleation mechanisms, to screen LVFFA-targeting aggregation inhibitors, and for aggregation kinetics. TFA powder; HFIP pre-treatment to aid dissolution; store long-term at −20°C. | In Alzheimer's disease (AD), misfolding and aggregation of amyloid-β (Aβ) into β-sheet oligomers and amyloid fibrils is a central pathological event. Numerous in vitro and computational studies show that residues 17–21, the central hydrophobic core (CHC) LVFFA, are the key site for intermolecular β-strand pairing, nucleation and fibril elongation, and are termed the Aβ 'self-recognition element' (SRE). This product, Aβ(16-22), comprises seven residues KLVFFAE and is the shortest self-aggregating model peptide containing LVFFA; after HFIP pre-treatment it spontaneously forms anti-parallel β-sheets, oligomers and fibrils in aqueous phase with a typical sigmoidal ThT curve, while its short, simple sequence makes it convenient for structural (NMR/IR/CD), kinetic and molecular-simulation studies. Its main uses include: (1) as a nucleation model to reveal β-sheet nucleation, homologous/heterogeneous seeding and oligomeric intermediates (e.g., β-barrel oligomers); (2) as a target model for aggregation inhibitors-many anti-aggregation small molecules and peptide inhibitors (e.g., iAβ5, KLVFF-derived peptides, aromatic compounds) block Aβ aggregation by binding/interfering with the LVFFA motif, and this peptide serves for high-throughput screening and mechanistic confirmation; (3) to study how solvent (HFIP, DMSO, pH, ionic strength), temperature and mutations affect the aggregation propensity of a minimal peptide; and (4) as a positive reference or co-aggregation seed for full-length Aβ40/Aβ42 aggregation assays. Because it nucleates rapidly and aggregates prematurely, strictly follow HFIP pre-treatment, prepare fresh solutions and keep on ice to ensure reproducibility. | Alzheimer's disease (AD), Aβ β-sheet nucleation mechanism, LVFFA central-hydrophobic-core model, minimal self-aggregating peptide, ThT aggregation-kinetics studies, anti-aggregation drug/peptide inhibitor screening model, amyloid fibril structure (NMR/CD/FTIR), molecular-simulation systems | No membrane receptor; targets the Aβ LVFFA motif itself for intermolecular interaction (self-aggregation/self-recognition motif) |
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