Beta-Amyloid (1-13)

Product Name: Beta-Amyloid (1-13)

Sequence One Letter Code: DAEFRHDSGYEVH

Sequence Three Letter Code: H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-OH

Chemical Formula:C67H92N20O24

Molecular Weight: 1561.7

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Alzheimer's Disease

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: β-Amyloid (1–13) is a synthetic peptide corresponding to the N-terminal residues 1–13 of the human amyloid-β sequence. This region contains important antigenic and hydrophilic determinants while lacking the hydrophobic C-terminal domain responsible for rapid fibril formation. Because of its improved solubility and defined antigenic properties, the fragment is widely used in immunological and biochemical studies examining amyloid recognition and early molecular interactions. The peptide is particularly useful for epitope mapping, antibody binding assays, and studies investigating immune responses to amyloid peptides. It also supports research into sequence-specific contributions to amyloid structure and function independent of mature fibril assembly. β-Amyloid (1–13) is commonly applied in Alzheimer’s disease research and immunogenicity studies.

Current Research: Introduction to N-Terminal Amyloid-β Fragments Amyloid-β (Aβ) peptides are central to Alzheimer’s disease research due to their role in aggregation, plaque formation, and neuronal dysfunction. These peptides originate from proteolytic processing of the amyloid precursor protein (APP) and can assemble into oligomers and fibrils associated with neurodegenerative pathology. To better understand the molecular features of amyloid peptides, researchers frequently examine shorter fragments that represent specific functional regions of the full sequence. β-Amyloid (1–13) is a synthetic peptide corresponding to the N-terminal residues 1–13 of the human amyloid-β sequence. This fragment retains important antigenic and structural characteristics of the N-terminal region while lacking the hydrophobic C-terminal segment responsible for rapid fibril formation. Structural Characteristics of the β-Amyloid (1–13) Fragment The N-terminal region of amyloid-β contains several hydrophilic and antigenic determinants that contribute to molecular recognition and interactions with antibodies and other proteins. In the β-Amyloid (1–13) fragment, these residues remain intact, preserving the key features required for immunological and biochemical studies. Unlike longer amyloid peptides such as Aβ1–40 or Aβ1–42, the 1–13 fragment does not contain the highly hydrophobic C-terminal domain that drives aggregation into fibrils. As a result, the peptide exhibits improved solubility and reduced aggregation tendency, allowing researchers to investigate molecular interactions without the complications of rapid fibril formation. This property makes β-Amyloid (1–13) particularly useful for experiments focusing on early amyloid interactions and sequence-specific biological properties. Applications in Epitope Mapping and Antibody Recognition One of the most important uses of the β-Amyloid (1–13) peptide is in epitope mapping studies. Because the N-terminal region contains antigenic sites recognized by many anti-amyloid antibodies, this fragment provides a convenient tool for identifying and characterizing antibody binding regions. Researchers commonly use this peptide in antibody binding assays to evaluate antibody specificity, affinity, and recognition patterns. By isolating the N-terminal segment of the amyloid sequence, scientists can determine which residues contribute most strongly to immune recognition. Such studies are essential for the development of diagnostic antibodies and therapeutic antibodies targeting amyloid-β peptides. Investigating Immune Responses to Amyloid Peptides The β-Amyloid (1–13) fragment is also widely used in immunological experiments investigating immune responses to amyloid peptides. Because it contains antigenic determinants without the aggregation-prone regions of the full peptide, it allows researchers to evaluate immune recognition under controlled conditions. In immunogenicity studies, the peptide can help researchers analyze how immune systems respond to specific amyloid sequences and how these responses influence antibody production. These investigations are particularly relevant for exploring immune-based approaches aimed at targeting amyloid pathology. Studying Early Amyloid–Protein Interactions Beyond immunological research, β-Amyloid (1–13) is also useful for studying early molecular interactions involving amyloid peptides. The N-terminal region participates in interactions with proteins, antibodies, and other biomolecules that influence amyloid behavior. Because the peptide remains relatively soluble and does not rapidly form fibrils, it provides a stable model for analyzing sequence-specific interactions independent of mature amyloid aggregation. Researchers can therefore investigate how individual residues contribute to amyloid structure and molecular recognition. These studies help clarify the initial stages of amyloid-related biochemical processes. Applications in Alzheimer’s Disease Research The β-Amyloid (1–13) peptide is widely applied in Alzheimer’s disease research, particularly in experiments focused on antibody recognition, immune responses, and early peptide interactions. Its defined length and antigenic properties allow researchers to analyze how specific regions of the amyloid sequence contribute to disease-related processes. In addition to immunological assays, the peptide may also be used in biochemical studies examining peptide conformation and molecular interactions associated with amyloid biology. Conclusion β-Amyloid (1–13) is a synthetic N-terminal fragment of the amyloid-β peptide that preserves key antigenic and hydrophilic determinants while lacking the aggregation-prone C-terminal domain. Its improved solubility and defined sequence make it a valuable tool for epitope mapping, antibody binding assays, and immunological studies of amyloid recognition. Widely used in Alzheimer’s disease research and immunogenicity studies, this peptide supports investigations into early amyloid–protein interactions and sequence-specific contributions to amyloid structure and function. By enabling focused analysis of the amyloid N-terminal region, β-Amyloid (1–13) remains an important reagent for studying amyloid biology and immune responses to amyloid peptides.