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| Description | GLMVGGVVIA (residues 33–42); the extra Ile-Ala (41–42) drives stronger hydrophobic packing and aggregation, making this TFA fragment a model for Aβ42 C-terminal-driven fibrillation. |
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 (33-42) (TFA) (human amyloid-β C-terminal residues 33–42, 10-mer, GLMVGGVVIA; pure hydrophobic C-terminal aggregation core) | Aβ(33-42) TFA; Amyloid β (33-42); GLMVGGVVIA; β-Amyloid (33-42) TFA salt | β-amyloid peptide, Aβ(33-42), Alzheimer's disease, C-terminal hydrophobic aggregation core, extremely aggregation-prone, very poor water solubility, fibrillation, neurotoxicity | Linear 10-mer; free N-terminal Gly and free C-terminal Ala carboxylic acid (-COOH); sequence Gly33-Leu-Met-Val-Gly-Gly-Val-Val-Ile-Ala42; the purely hydrophobic C-terminal region of Aβ, composed only of Gly/Leu/Val/Ile/Met with no charged residues; the key C-terminal hydrophobic core driving the strong aggregation and fibril stabilization of Aβ(1-42) | C41H74N10O11S (free acid) | 1028.5 | 1029.18 | TFA salt (Trifluoroacetate) | 10 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-AB3342T-01 | White to off-white powder | Store at −20°C, sealed, desiccated, protected from light; aliquot to avoid repeated freeze-thaw, ~1–2 years. This purely hydrophobic C-terminal 10-mer aggregates/fibrillizes extremely readily and may aggregate slowly even in the solid state; immediate HFIP pre-treatment and aliquoting upon receipt are recommended. | 2–8°C for ≤1 week; working aliquots must be stored at −80°C; avoid room-temperature exposure; ship on dry ice. | Purely hydrophobic C-terminal 10-mer with very poor water solubility; aggregates extremely readily into oligomers/fibrils. Handle strictly by protocol: resuspend powder in hexafluoroisopropanol (HFIP) at 1–2 mM, sonicate/vortex to disrupt pre-aggregates, dry under nitrogen, reconstitute in DMSO then dilute into buffer. Solution stability at 4°C is very poor; aliquot and store at −80°C; avoid repeated freeze-thaw. | solid stable for ~1–2 years at −20°C, sealed, desiccated, protected from light; contains oxidizable Met, so store dry, protected from light, under inert gas; HFIP pre-treatment and immediate aliquoting upon receipt to disrupt pre-aggregates. |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Receptors |
| PEP-AB3342T-01 | Human Aβ(33-42) TFA salt 10-mer (GLMVGGVVIA), the pure hydrophobic C-terminal aggregation core; extremely aggregation-prone with very poor water solubility; used for AD C-terminal-driven fibrillation/neurotoxicity studies; white powder requiring HFIP/DMSO pre-treatment and −80°C aliquots. | The C-terminal hydrophobic region of amyloid-β (approximately residues 30–42) is the key structural basis why Aβ(1-42) aggregates faster and is more neurotoxic than Aβ(1-40). Aβ(33-42) spans Gly33 to Ala42 (GLMVGGVVIA), composed entirely of hydrophobic amino acids (Gly, Leu, Met, Val, Ile, Ala) with no charged residues, representing the purest hydrophobic aggregation core of the Aβ(1-42) C-terminus. Despite its short length, this fragment retains a strong self-aggregation propensity and rapidly assembles in aqueous phase into β-sheet-rich oligomers and fibrils with strong Thioflavin T fluorescence. Its C-terminal Ala42 is one of the two extra residues (Ile41-Ala42) that distinguish Aβ(1-42) from Aβ(1-40), and is thought to enhance C-terminal hydrophobic packing, stabilize fibrils and increase neurotoxicity. Due to its extremely poor water solubility, this peptide must be pre-treated with HFIP/DMSO before use. It is widely used to: study the role of the C-terminal hydrophobic region in Aβ fibrillation and fibril stabilization; compare C-terminal differences between Aβ(1-42) and Aβ(1-40); screen anti-aggregation inhibitors targeting the C-terminal hydrophobic core; and serve as a standardized hydrophobic aggregation model peptide for ThT kinetics, EM/AFM morphology and membrane-toxicity studies. | Alzheimer's disease (AD), Aβ C-terminal hydrophobic aggregation core, fibrillation/fibril stabilization, Aβ(1-42) vs Aβ(1-40) differences, neurotoxicity/membrane damage, anti-aggregation drug screening, ThT kinetics and fibril morphology (EM/AFM) | Aβ C-terminal hydrophobic self-aggregation (monomer → oligomer → fibril); the C-terminal 33–42 hydrophobic core is an anti-aggregation inhibitor target; I41-A42 enhances fibril stability and neurotoxicity |
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