Beta-Amyloid (1-15)

Product Name: Beta-Amyloid (1-15)

Sequence One Letter Code: DAEFRHDSGYEVHHQ

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

Cas No: 183745-81-5

Chemical Formula:C78H107N25O27

Molecular Weight: 1827

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Alzheimer's Disease

SMILES: C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC2=CNC=N2)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC3=CC=C(C=C3)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC4=CNC=N4)C(=O)N[C@@H](CC5=CNC=N5)C(=O)N[C@@H](CCC(=O)N)C(=O)O)NC(=O)[C@H](CC(=O)O)N

IUPAC: (2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]propanoyl]amino]-4-carboxybutanoyl]amino]-3-phenylpropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-4-carboxybutanoyl]amino]-3-methylbutanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-5-oxopentanoic acid

INCHIKEY: CSCAPVBQOYQJJF-NOZGEEMHSA-N

INCHI:

InChI=1S/C78H107N25O27/c1-37(2)63(76(128)101-54(26-43-31-85-36-90-43)74(126)99-52(24-41-29-83-34-88-41)72(124)96-49(77(129)130)15-18-57(80)106)103-69(121)48(17-20-60(110)111)95-70(122)50(23-40-11-13-44(105)14-12-40)92-58(107)32-87-66(118)56(33-104)102-75(127)55(28-62(114)115)100-73(125)53(25-42-30-84-35-89-42)98-67(119)46(10-7-21-86-78(81)82)94-71(123)51(22-39-8-5-4-6-9-39)97-68(120)47(16-19-59(108)109)93-64(116)38(3)91-65(117)45(79)27-61(112)113/h4-6,8-9,11-14,29-31,34-38,45-56,63,104-105H,7,10,15-28,32-33,79H2,1-3H3,(H2,80,106)(H,83,88)(H,84,89)(H,85,90)(H,87,118)(H,91,117)(H,92,107)(H,93,116)(H,94,123)(H,95,122)(H,96,124)(H,97,120)(H,98,119)(H,99,126)(H,100,125)(H,101,128)(H,102,127)(H,103,121)(H,108,109)(H,110,111)(H,112,113)(H,114,115)(H,129,130)(H4,81,82,86)/t38-,45-,46-,47-,48-,49-,50-,51-,52-,53-,54-,55-,56-,63-/m0/s1

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: β-Amyloid (1–15) corresponds to the N-terminal fragment of the human amyloid-β peptide spanning residues 1–15. This region contains key antigenic and hydrophilic determinants involved in early amyloid interactions while lacking the highly aggregation-prone C-terminal segment. Because of its improved solubility and defined antigenic properties, the peptide is frequently used to study antibody recognition, epitope mapping, and immune responses to amyloid peptides. It also supports investigations into early amyloid–protein interactions independent of fibril formation. The fragment is widely applied in biochemical, structural, and immunological assays related to Alzheimer’s disease research. Its defined length allows researchers to examine sequence-specific contributions to amyloid antigenicity, molecular interactions, and mechanisms involved in amyloid-associated pathology.

Current Research: Overview of the Amyloid-β N-Terminal Region Amyloid-β (Aβ) peptides are central to the molecular pathology of Alzheimer’s disease and are widely studied for their role in plaque formation, neuronal toxicity, and neurodegenerative signaling pathways. These peptides are generated through enzymatic cleavage of the amyloid precursor protein (APP) and can assemble into oligomers and fibrillar aggregates within neural tissues. To better understand the molecular properties of amyloid peptides, researchers often investigate shorter fragments representing specific regions of the full sequence. β-Amyloid (1–15) is a synthetic peptide corresponding to the N-terminal residues 1–15 of the human amyloid-β sequence. This fragment preserves important antigenic and structural features of the N-terminal domain while avoiding the highly aggregation-prone C-terminal region. Structural Characteristics of the 1–15 Fragment The β-Amyloid (1–15) fragment contains several hydrophilic residues and antigenic determinants located within the N-terminal region of the full amyloid-β peptide. These residues contribute to molecular recognition and early peptide interactions. Unlike longer amyloid fragments such as Aβ1–40 or Aβ1–42, the 1–15 segment lacks the hydrophobic C-terminal domain that drives rapid aggregation and fibril formation. As a result, the peptide exhibits improved solubility and reduced aggregation tendency under experimental conditions. This property makes β-Amyloid (1–15) particularly suitable for studies that focus on early molecular events in amyloid biology without interference from rapid fibril assembly. Antigenic Determinants and Antibody Recognition The N-terminal region of amyloid-β contains several antigenic epitopes recognized by antibodies targeting amyloid peptides. Because β-Amyloid (1–15) includes these determinants, it is widely used in experiments investigating antibody recognition and antigen–antibody interactions. Synthetic peptides representing this region are frequently used in antibody binding assays, epitope mapping studies, and immunological experiments designed to identify antibody recognition sites within amyloid-β. By isolating the N-terminal sequence, researchers can analyze how antibodies interact with specific peptide motifs and determine which residues contribute most strongly to immune recognition. These studies are valuable for developing diagnostic antibodies and evaluating antibody-based therapeutic approaches targeting amyloid peptides. Applications in Epitope Mapping and Immunological Studies Because of its defined antigenic properties, β-Amyloid (1–15) is commonly applied in epitope mapping and immunogenicity testing. In these experiments, the peptide is used to determine which segments of amyloid-β are recognized by specific antibodies or immune receptors. Epitope mapping studies are particularly important for understanding immune responses to amyloid peptides and for guiding the design of immunotherapies aimed at reducing amyloid accumulation. By using a defined N-terminal fragment, researchers can identify the structural elements responsible for antibody binding and evaluate how sequence variations influence immune recognition. The peptide therefore plays a useful role in studies exploring immune responses to amyloid peptides in Alzheimer’s disease models. Investigating Early Amyloid–Protein Interactions In addition to immunological applications, β-Amyloid (1–15) supports investigations into early amyloid–protein interactions. Because the fragment lacks the hydrophobic region responsible for rapid fibril formation, it allows researchers to examine how the N-terminal domain interacts with other biomolecules in solution. These interactions may include binding with proteins, antibodies, metal ions, or other ligands that influence amyloid structure and biological activity. Studying these interactions helps clarify how amyloid peptides behave before the onset of large-scale aggregation. Such experiments provide insight into the initial molecular events associated with amyloid formation and amyloid-related cellular responses. Applications in Alzheimer’s Disease Research The β-Amyloid (1–15) peptide is widely used in biochemical, structural, and immunological assays related to Alzheimer’s disease research. Its defined length and improved solubility make it a convenient model system for studying the antigenic and structural features of the amyloid N-terminal domain. Researchers often use this fragment to evaluate antibody recognition patterns, investigate molecular interactions involving amyloid peptides, and analyze sequence-specific contributions to amyloid antigenicity. These studies help clarify how different regions of the amyloid peptide contribute to disease-related processes. Conclusion β-Amyloid (1–15) is an N-terminal fragment of the human amyloid-β peptide that preserves key antigenic and structural features while lacking the aggregation-prone C-terminal region. Its hydrophilic nature and defined sequence make it particularly useful for antibody recognition studies, epitope mapping, and investigations of early amyloid–protein interactions. Widely applied in biochemical and immunological assays, this peptide supports research exploring amyloid antigenicity, molecular interactions, and mechanisms involved in Alzheimer’s disease–associated pathology. By enabling focused analysis of the amyloid N-terminal domain, β-Amyloid (1–15) continues to serve as an important tool in amyloid and neurodegenerative disease research.