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| Description | QKLVFFA (residues 15–21) self-assembles into β-sheet fibrils; a minimal model for amyloid nucleation, intermolecular β-sheet packing and KLVFF-targeting inhibitors. |
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) |
| beta-Amyloid (15-21), human (QKLVFFA, 7-mer, contains LVFFA hydrophobic core) | Aβ(15-21); QKLVFFA; β-Amyloid 15-21; Gln-Lys-Leu-Val-Phe-Phe-Ala | β-amyloid peptide, Aβ fragment, LVFFA hydrophobic core, aggregation core segment, Alzheimer's disease (AD), Aβ aggregation/fibrillization model, aggregation inhibitor screening, ThT assay | Linear 7-mer: Gln-Lys-Leu-Val-Phe-Phe-Ala (QKLVFFA), corresponding to human Aβ residues 15 (Gln) through 21 (Ala); contains the LVFFA (17-21) hydrophobic aggregation core; free N-terminal Gln and free C-terminal Ala-OH. | C43H65N9O9 | 851.49 | 852.05 | Free acid (C-terminal -COOH); TFA/acetate forms available on request; CAS 365537-52-6 | 7 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-BAβ15-21-01 | White powder | Store at -20°C, sealed and desiccated; aliquot to avoid repeated freeze-thaw cycles; ~2 years shelf life. The hydrophobic LVFF segment may slowly aggregate even in the solid state; keep dry. | Short-term storage at 2–8°C for up to ~2 weeks; prepare working solutions fresh; avoid prolonged room-temperature exposure. | Moderately good water solubility (polar N-terminal Gln/Lys) but the C-terminal LVFFA is strongly hydrophobic; dissolve with a small amount of DMSO or suitable buffer. Once dissolved, stable short-term at 4°C; store aliquots at -20°C. Peptide tends to aggregate in solution-use fresh and avoid repeated freeze-thaw. | solid is stable for ~2 years at -20°C, sealed and desiccated. Hygroscopic; upon caking/aggregation, use promptly and store under inert gas after opening. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-BAβ15-21-01 | Human Aβ(15-21) 7-mer QKLVFFA containing the LVFFA hydrophobic core; a classic short-peptide model for studying the Aβ aggregation core and screening anti-aggregation agents. | β-Amyloid (15-21) corresponds to the central hydrophobic core of human Aβ (QKLVFFA). The Leu-Val-Phe-Phe-Ala segment (LVFFA, residues 17-21) is the key recognition motif driving Aβ self-assembly, β-sheet formation and fibril elongation. Numerous in vitro studies show that KLVFF (16-20) and the longer 15-21 segment themselves aggregate into β-sheet-rich assemblies and can act as dominant-negative decoys that bind full-length Aβ(1-40/1-42) and inhibit fibrillization. This fragment is widely used for: (1) structural and mechanistic studies of the Aβ core aggregation region; (2) structure-activity relationship studies of small-molecule/peptide aggregation inhibitors targeting LVFFA; (3) model peptide in ThT fluorescence aggregation assays; (4) co-incubation interference experiments with full-length Aβ. Because it is short and readily synthesized and modified, 15-21 also serves as a parent scaffold for PEGylation, cyclization, D-amino acid substitution and other anti-aggregation drug-design strategies. | Alzheimer's disease (AD), Aβ aggregation mechanism, LVFFA hydrophobic core, aggregation inhibitor screening, ThT fluorescence assay, β-sheet/fibril formation, peptide-based anti-aggregation drug design | Aβ self-aggregation (monomer → oligomer → β-sheet → fibril); dominant-negative binding to full-length Aβ(1-40/1-42); LVFFA hydrophobic-core interface |
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