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| Description | MVGGVVIA (residues 35–42), the Aβ42-specific C-terminus with hydrophobic Ile-Ala (41–42); the key C-terminal determinant of Aβ42's stronger aggregation and toxicity. |
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) |
| β-Amyloid (35-42) human TFA, CAS 183292-41-3 (human Aβ C-terminal 35-42 nonapeptide fragment, TFA salt; sequence MLVGGVVIA, contains oxidizable Met35) | Aβ(35-42); C-terminal hydrophobic fragment; MLVGGVVIA; Aβ C-terminal hydrophobic octapeptide | β-amyloid peptide, C-terminal hydrophobic fragment, highly hydrophobic, C-terminal aggregation core, oxidizable Met35, short-peptide aggregation model, membrane-insertion study | Linear 9-mer, pure C-terminal hydrophobic segment MLVGGVVIA, spanning Met35-Leu-Val-Gly-Gly-Val-Val-Ile-Ala; contains the strongly hydrophobic GGVVIA core that drives the monomer-to-β-sheet/fibril transition; includes oxidizable Met35 (readily oxidized to MetO) | C39H71N9O10S1 | 857.50 | 858.11 | TFA salt / powder; CAS 183292-41-3 | 9 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Stability |
| PEP-AB3542-01 | White to off-white powder | Store at −20°C, sealed, desiccated, protected from light; aliquot into single-use portions to avoid repeated freeze-thaw, ~2 years; contains oxidizable Met35, storage under argon/nitrogen preferred. | 2–8°C for ~1 week; working aliquots at −80°C; avoid room-temperature exposure; ship on dry ice/blue ice. | Poorly water-soluble; first dissolve in DMSO or hexafluoroisopropanol (HFIP) at 1–2 mM, then dilute with PBS/buffer to the desired concentration; keep solutions at 4°C for ≤24 h or aliquot and store at −80°C; avoid repeated freeze-thaw; Met35 is readily oxidized to MetO-prepare fresh and keep under argon. | solid stable for ~2 years at −20°C, sealed, desiccated and protected from light; highly hygroscopic and aggregation-prone, store dry under inert gas, protected from light; contains oxidizable Met35, keep dark, dry and at −20°C. |
Functional Description
| Product Code | Short Summary (listing) | Detailed Biological Function | Research Areas | Targets/Receptors |
| PEP-AB3542-01 | Human Aβ C-terminal 35-42 nonapeptide hydrophobic fragment (TFA salt, CAS 183292-41-3), sequence MLVGGVVIA, containing the strongly hydrophobic GGVVIA core and oxidizable Met35. This C-terminal region is critical for the monomer-to-β-sheet/fibril transition; the peptide itself shows strong self-aggregation propensity and is used to study C-terminal hydrophobic interactions, membrane insertion, the effect of Met35 oxidation on aggregation, and as a short-peptide aggregation model. Poorly water-soluble; requires DMSO/HFIP cosolvent. | The C-terminus of Aβ(1-42) (residues 28-42, KGAIIGLMVGGVVIA) is a highly hydrophobic, transmembrane-like α-helical segment widely recognized as the core region driving the transition of Aβ monomers into β-sheet oligomers and fibrils. Residues 35-42 (Met35-Val-Gly-Gly-Val-Val-Ile-Ala) lie at the very C-terminal end and contain the extremely hydrophobic Gly-Gly-Val-Val-Ile-Ala (GGVVIA) repeat, a key contact region for intermolecular hydrophobic interactions, β-sheet stacking and fibril-core formation. Crystallographic and solid-state NMR studies show that in Aβ fibrils the GGVVIA segment forms a tightly packed β-sheet hydrophobic interface, with aromatic residues (Phe19/20) and the C-terminal hydrophobic segment jointly constituting the amyloid core. Aβ(35-42) (MLVGGVVIA), as the minimal short-peptide model of this C-terminal core, itself shows strong self-aggregation and can form β-sheet fibril-like structures, making it a classic model peptide for studying short-peptide amyloid aggregation, C-terminal hydrophobic interactions and membrane insertion. In addition, the N-terminal Met35- the only methionine in Aβ-is readily oxidized to methionine sulfoxide (MetO35) under the oxidative stress environment of AD brain; Met35 oxidation alters C-terminal hydrophobicity and conformation, in turn affecting Aβ aggregation rate, membrane interaction and neurotoxicity. Aβ(35-42) is therefore also widely used as: an in vitro model of how the Met35 redox state affects Aβ aggregation; a tool for C-terminal hydrophobic interaction and membrane insertion / detergent-micelle interaction studies; a simplified model for short-peptide amyloid aggregation kinetics (ThT, CR, CD); and a substrate for screening and mechanistic studies of Aβ aggregation inhibitors, particularly small-molecule/peptide inhibitors targeting the C-terminal hydrophobic core. Supplied as TFA-salt powder with poor water solubility; first dissolve in DMSO or HFIP, then dilute with buffer. | Alzheimer's disease (AD), Aβ C-terminal hydrophobic aggregation, Met35 oxidation and aggregation, membrane interaction/insertion, short-peptide aggregation model, amyloid core GGVVIA, C-terminal-targeted aggregation-inhibitor screening | Aβ self-aggregation (C-terminal hydrophobic core GGVVIA); Met35 redox site; membrane bilayer / detergent-micelle insertion |
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