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| Description | Introduces negatively charged Asp into the hydrophobic C-terminal packing at residue 37, disrupting hydrophobic packing; used to dissect the role of the C-terminal core in Aβ42 oligomerization and fibril stability. |
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) |
| (Asp37)-Amyloid β-Protein (1-42) | G37D Aβ(1-42); Gly37→Asp Aβ42; C-terminal charge-mutant Aβ42; Aβ42-G37D | C-terminal G37D mutation, charged residue in transmembrane region, altered C-terminal conformation/membrane insertion, aggregation- and toxicity-modulating charge scan, strong aggregation / mandatory HFIP | Linear 42-mer, sequence DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVDGVVIA (human Aβ residues 1–42; Gly37→Asp, G37D). Free N-terminal amine and free C-terminal carboxylate (non-amidated); contains one Met35. Wild-type residues 35–42 (MLVGGVVIA) form a highly hydrophobic transmembrane-like C-terminal segment that drives fibril elongation after beta-sheet nucleation and membrane insertion. G37D introduces a negatively charged Asp side chain into this hydrophobic region, locally altering electrostatics and conformation-C-terminal dihedral angles, beta-strand packing and membrane insertion/interfacial behavior-and thereby modulating the aggregation pathway, oligomer composition and neurotoxicity of Aβ42. Strongly aggregating; HFIP de-aggregation is mandatory before use. | C205H313N55O62S | 4569.28 | 4572.14 | TFA salt; CAS 1875128-79-2 | 42 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Stability |
| PEP-ABD37-01 | White to off-white powder | Store at −20°C, sealed, desiccated, protected from light; aliquot under argon/nitrogen; avoid repeated freeze-thaw; ~2 years. | Brief shipping/storage at 2–8°C (~1 week); keep working solutions on ice and aliquot for −80°C; ship on dry ice or ample blue ice. | G37D introduces a negative charge into the hydrophobic C-terminal transmembrane region, altering C-terminal conformation and membrane-insertion propensity, but the full-length Aβ42 backbone still aggregates strongly. **HFIP de-aggregation is mandatory**: dissolve the lyophilate in HFIP (~1–2 mM), sonicate on ice 5–10 min, aliquot and evaporate to a monomeric film under vacuum, store at −20°C; before use, dissolve in dilute NaOH (~pH 10) then neutralize to pH 7.4, or reconstitute the HFIP film in pH 7.4 PBS and use fresh on ice. Do not keep solutions at room temperature; avoid repeated freeze-thaw. When comparing aggregation kinetics, monomerize this mutant and wild-type Aβ42 in the same batch under identical conditions. | solid stable ~2 years at −20°C, sealed, desiccated, light-protected, under inert gas; hygroscopic-keep dry/dark/sealed; contains oxidizable Met35, minimize repeated opening. |
Functional Description
| Product Code | Short Summary (listing) | Detailed Biological Function | Research Areas | Targets/Receptors |
| PEP-ABD37-01 | Human Aβ(1-42) with Gly37→Asp (G37D), 42-mer. Introduces a single negative charge into the highly hydrophobic C-terminal transmembrane segment (MLVGGVVIA), altering local C-terminal conformation, beta-strand packing and membrane-insertion behavior. A tool peptide for studying how C-terminal charge modulates the aggregation pathway, oligomer composition and neurotoxicity of Aβ42. HFIP de-aggregation mandatory; use fresh. | The C terminus of Aβ42 (~residues 29–42, GAIIGLMVGGVVIA) is a highly hydrophobic transmembrane-like sequence: residues 30–36 (KGAIIGL) form a second hydrophobic core, and residues 35–42 (MLVGGVVIA) insert into membranes and, after beta-sheet formation, drive fibril elongation and interfacial binding. The conformational and hydrophobic balance of the C terminus is considered key to why Aβ42 aggregates faster and is more toxic than Aβ40-the two extra residues Ile41-Ala42 in Aβ42 markedly raise the nucleation rate. Replacing a point in this hydrophobic region with a charged residue (G37D)-inserting an anionic Asp at a position that is otherwise side-chain-free Gly-locally perturbs the C-terminal electrostatic environment, beta-strand dihedrals and the helix/sheet conformational equilibrium without changing length, thereby altering: (1) nucleation and elongation kinetics; (2) secondary-structure composition of oligomers/fibrils; (3) insertion and solubilization behavior with lipid vesicles and plasma membranes; and (4) subsequent neurotoxicity. This G37D Aβ42 is a site-directed tool peptide for studying how C-terminal charge controls Aβ42 aggregation and membrane toxicity; it is typically paired with wild-type Aβ42, Aβ40 and other C-terminal variants (e.g. G37A, M35-oxidized analogs) in ThT aggregation-kinetics, CD/FTIR secondary-structure, DLS, TEM/AFM morphology, liposome-leakage and cell-cytotoxicity comparisons. Note: despite the introduced charge, the 42-mer backbone still aggregates rapidly-always monomerize with HFIP; contains Met35, protect from oxidation. | Aβ42 C-terminal charge-scanning mutant, transmembrane hydrophobic-region membrane-insertion mechanism, C-terminal conformation/beta-sheet regulation, comparative aggregation kinetics, oligomer/fibril structure, liposome/plasma-membrane interaction, neurotoxicity mechanism, structure-relationship tool peptide | Aβ self-aggregation / beta-sheet fibrils; inserts into and perturbs lipid bilayers/plasma membranes; no specific receptor target; used as a C-terminal conformation-aggregation model |
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