N3-Lys-Amyloid Beta 1-42 Peptide

N3-Lys-Amyloid Beta 1-42 Peptide is derived from the amyloid-beta sequence generated from human amyloid-beta precursor protein (APP). The canonical Aβ region is publicly curated within human APP UniProtKB entry P05067.

Amyloid Beta Research Peptides

Amyloid-beta peptides are central research reagents in studies of peptide aggregation, amyloid fibril formation, membrane interactions, proteolytic processing, antibody recognition, and analytical assay development. Aβ1-40 and Aβ1-42 are the two most widely studied C-terminal forms.

Aβ1-42 contains two additional C-terminal residues relative to Aβ1-40 and generally displays stronger aggregation propensity under many experimental conditions. Sequence, concentration, solvent history, pre-treatment, and incubation conditions can all strongly affect aggregation state.

Aβ1-42 Parent Sequence

DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

N-Terminal Azido-Lysine Handle

LT8744 contains the complete Aβ1-42 sequence preceded by an added Lys(N3) residue. The azide functionality provides a site for click-chemistry conjugation while leaving all 42 residues of the canonical Aβ sequence present in the construct.

The added lysine is not part of native Aβ1-42 and can influence physicochemical behavior; application-specific validation is recommended.

Potential Research Applications

• Amyloid aggregation studies
• LC-MS analytical methods
• Antibody binding assays
• Peptide-protein interaction studies
• Fluorescent or chemical conjugation
• Reference-standard development

For aggregation-sensitive studies, peptide handling and pre-treatment procedures should be standardized across experiments.

References

UniProt Consortium APP - Amyloid-beta precursor protein - Homo sapiens. UniProtKB P05067.
Public source / publication

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Research Use Only. Not for human, diagnostic, clinical, or therapeutic use.

N3-Lys-Amyloid Beta 1-42 Peptide is a synthetic amyloid-beta (Aβ) research peptide. Amyloid-beta peptides are proteolytic products of amyloid precursor protein. Sequence length and residue composition strongly influence aggregation: Aβ42 generally aggregates more rapidly than Aβ40, and C-terminal fragments containing residues in the 34-42 region can adopt stable beta-structure. Truncated, reverse-sequence, isotopically labeled, or chemically modified Aβ constructs are therefore best interpreted as distinct research reagents rather than assumed equivalents of native Aβ40 or Aβ42.

• amyloid aggregation and fibrillization studies
• LC-MS/HPLC analytical reference work
• Aβ sequence-length and modification comparisons
• antibody, binding, and assay controls

The exact sequence, phosphorylation state, residue numbering, terminal modifications, labels, and species context should be matched to the intended assay. Sequence motifs support experimental interpretation but do not by themselves establish absolute enzyme specificity or native biological activity.

1. Sequence determinants of enhanced amyloidogenicity of Aβ42 relative to Aβ40
2. Molecular determinants of amyloid deposition: synthetic beta-protein fragments
3. Impact of sequence on assembly of short amyloid peptides