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| Description | QKLVFF (residues 15–20) with blocked termini to remove end-charge effects; KLVFF is the self-recognition core, used for short-peptide self-assembly and KLVFF-targeting inhibitors. |
Product Basic Information Table
| Standard English Name | Abbreviations/Aliases | Functional Tags | Structural Core | Molecular Formula | Exact MW (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Acetyl-β-Amyloid (15-20), Amide (human N-acetylated, C-amidated amyloid-β residues 15–20, 6-mer, Ac-QKLVFF-NH2; CAS 189064-06-0) | Ac-Aβ(15-20)-NH2; Ac-QKLVFF-NH2; Aβ(15-20) amide; LVFFA-core upstream short peptide; acetylated Aβ15-20 | β-amyloid fragment, Aβ(15-20), LVFFA hydrophobic-core upstream, N-acetylation, C-amidation, terminal charge shielding, membrane-mimetic stabilization, short-peptide epitope, non-fibrillizing/water-soluble, membrane-interaction model, aggregation-core study | Linear hexapeptide Ac-Gln15-Lys16-Leu17-Val18-Phe19-Phe20-NH2, i.e. Aβ(15-20)=QKLVFF; the N-terminal Gln15 amino group is acetylated (Ac-) and the C-terminal Phe20 carboxyl group is amidated (-NH2), so neither terminus carries charge, mimicking neutral termini under physiological/membrane-mimetic conditions; immediately upstream of the Aβ central hydrophobic core LVFFA (17–21), containing Leu17-Val18-Phe19-Phe20 aromatic/hydrophobic residues; the short peptide does not form β-sheets or fibrils and is water-soluble, commonly used for upstream-core epitope mapping and peptide-membrane interaction models | C42H63N9O8 | 821.48 | 822.02 | TFA/acetate powder; CAS 189064-06-0 | 6 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Stability |
| PEP-AB1520-01 | White to off-white powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~2 years. The short peptide is stable and non-aggregating; routine dry cold storage suffices. | 2–8°C for ~1 week; working aliquots at −20°C; avoid prolonged room-temperature exposure; ship on blue ice (ambient acceptable). | The short peptide is water-soluble and can be reconstituted directly in deionized water, PBS or buffer-no HFIP pretreatment needed; terminal charges are shielded by acetylation/amidation, giving more stable conformations under membrane-mimetic conditions (DMPC/SDS micelles/liposomes) and avoiding charged-terminal extreme aggregation; it does not form β-sheets/fibrils. Solutions keep for a few days at 4°C; prepare fresh and aliquot/store at −20°C. | solid stable for ~2 years at −20°C, sealed and desiccated; hygroscopic, store dry and protected from light; no oxidizable Met, good stability. |
Functional Description
| Product Code | Short Summary (listing) | Detailed Biological Function | Research Areas | Targets/Receptors |
| PEP-AB1520-01 | Human Aβ(15-20)=QKLVFF hexapeptide, N-terminally acetylated (Ac-) and C-terminally amidated (-NH2) to shield terminal charges and improve stability under membrane-mimetic conditions (CAS 189064-06-0). It lies immediately upstream of the Aβ central hydrophobic core LVFFA (17–21) and contains the Leu-Val-Phe-Phe aromatic/hydrophobic sequence-a classic short-peptide model for studying the upstream epitope of the Aβ aggregation core, short-peptide–membrane interactions and anti-Aβ antibody epitopes. Water-soluble, non-fibrillizing and non-aggregating; reconstitute directly in buffer. White to off-white powder. | The key driving force of Aβ aggregation resides in the central hydrophobic core (CHC), residues 17–21 (LVFFA); the aromatic stacking (π–π interaction) of Phe19–Phe20 is a critical molecular basis for β-sheet nucleation and fibrillation. Aβ(15-20)=Gln15-Lys16-Leu17-Val18-Phe19-Phe20 (QKLVFF) covers exactly the upstream boundary of the LVFFA core and the key aromatic residues, and is a widely used short-peptide model for studying how upstream sequences of the nucleation region modulate aggregation and for mapping anti-Aβ antibody epitopes. This product acetylates the N-terminal Gln15 (Ac-) and amidates the C-terminal Phe20 (-NH2), shielding the net charge at both termini-at physiological pH a free N-terminal amino group is positive and a free C-terminal carboxyl group is negative, causing strong electrostatic interactions on the membrane surface and confounding conformational interpretation; terminal shielding makes the short peptide more closely resemble the charge-free terminal state after insertion into membranes/micelles, improving conformational stability and reproducibility under membrane-mimetic conditions (SDS/DPC micelles, DMPC/DMPG liposomes, dodecylphosphocholine). Because it is only six residues long and cannot extend long-range β-sheets, Ac-QKLVFF-NH2 itself does not form fibrils, does not aggregate spontaneously and is water-soluble; it is commonly used as: (1) the LVFFA-core upstream short peptide/epitope to map the binding epitopes of anti-Aβ antibodies (e.g. mAbs targeting the central core region); (2) a simplified short-peptide–membrane interaction model to study how aromatic/hydrophobic residues drive peptide insertion into phospholipid membranes and induce membrane perturbation/ion channels; (3) a binding target/control peptide for aggregation inhibitors (molecular recognition elements, aromatic small molecules, cyclic peptides); (4) a minimal peptide representing the CHC upstream fragment for NMR, circular dichroism (CD) and molecular-dynamics simulations. Since it does not fibrillize, its aggregation behavior should not be directly equated with full-length Aβ(1-40/42); it is suited as a tool for epitope and membrane-interaction studies. | Alzheimer's disease (AD), Aβ central hydrophobic core LVFFA study, aggregation-nucleation upstream sequences, short-peptide epitope mapping, anti-Aβ antibody epitope mapping, peptide-membrane interaction/ion-channel models, aggregation-inhibitor screening control, NMR/CD conformational studies, terminal-charge shielding in membrane mimetics | Aβ central hydrophobic core LVFFA (17–21) upstream QKLVFF segment; Phe19–Phe20 aromatic π–π stacking nucleation element; N-terminal Ac / C-terminal -NH2 shielding terminal charges; short-peptide model for anti-central-core antibodies and aggregation inhibitors |
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