Beta-Amyloid (17-24)

Product Name: Beta-Amyloid (17-24)

Sequence One Letter Code: LVFFAEDV

Sequence Three Letter Code: H-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-OH

Chemical Formula:C46H66N8O13

Molecular Weight: 939.1

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 (17–24) corresponds to a central region of the amyloid-β peptide that plays a key role in aggregation and fibril formation. Residues within this segment contribute to the structural transition from α-helical conformations to β-strand structures during amyloid assembly. Because of its involvement in nucleation and intermolecular interactions, this fragment is widely used in studies examining the mechanisms of amyloid fibrillogenesis. The peptide supports structural and biophysical investigations focused on peptide folding, intermolecular interactions, and early stages of aggregation. It is commonly applied in Alzheimer’s disease research to dissect sequence-specific determinants that drive amyloid formation. The fragment also supports screening efforts aimed at identifying molecules capable of modulating amyloid aggregation.

Current Research: Introduction to Amyloid Aggregation in Alzheimer’s Disease Amyloid-β (Aβ) peptides are closely associated with the pathology of Alzheimer’s disease, where their aggregation into oligomers and fibrillar deposits contributes to neuronal dysfunction and neurodegeneration. Understanding the molecular mechanisms that drive amyloid aggregation is a major focus of biochemical and structural research. To investigate the specific sequence elements responsible for amyloid assembly, researchers often study short peptide fragments derived from the full-length amyloid-β sequence. One such fragment is β-Amyloid (17–24), which represents a central region of the peptide known to play a critical role in aggregation and fibril formation. Structural Significance of the 17–24 Region The β-Amyloid (17–24) fragment corresponds to a central segment of the amyloid-β peptide that contains residues strongly associated with aggregation behavior. This region is part of the hydrophobic core that contributes to intermolecular interactions during amyloid assembly. Within this sequence, amino acids facilitate the transition of amyloid peptides from soluble conformations into ordered β-sheet structures. These structural changes are essential for the formation of amyloid fibrils, which are characteristic features observed in Alzheimer’s disease pathology. Because of its structural importance, the 17–24 region is frequently studied as a model system for understanding the molecular determinants of amyloid aggregation. Conformational Transitions During Amyloid Assembly One of the defining features of amyloid formation is the structural transition from α-helical or disordered conformations to β-strand-rich structures. This conformational change enables peptides to align and stack into β-sheet assemblies that ultimately form fibrillar aggregates. Residues within the β-Amyloid (17–24) fragment play an important role in promoting this transition. The segment participates in intermolecular interactions that stabilize β-sheet structures, supporting the nucleation and elongation phases of amyloid fibril formation. Because of this behavior, the peptide provides researchers with a simplified model for examining how structural rearrangements contribute to amyloid assembly. Applications in Amyloid Fibrillogenesis Studies The β-Amyloid (17–24) fragment is widely used in biophysical and structural studies investigating amyloid fibrillogenesis. Researchers employ this peptide to analyze how individual residues and sequence motifs contribute to peptide folding and aggregation dynamics. Experimental techniques such as spectroscopy, microscopy, and structural modeling can be applied to examine how this central segment interacts with itself or with other peptide molecules during aggregation. By focusing on this defined sequence, scientists can dissect the molecular interactions responsible for amyloid nucleation and fibril growth. These studies help clarify the mechanisms that drive amyloid assembly at the molecular level. Investigating Intermolecular Interactions and Peptide Folding Because β-Amyloid (17–24) represents a key aggregation motif, it is frequently used in experiments exploring intermolecular interactions between amyloid peptides. The fragment allows researchers to analyze how hydrophobic contacts and structural alignment contribute to β-sheet formation. In addition, the peptide is useful for studying peptide folding and conformational stability. By isolating this aggregation-prone region, researchers can examine how environmental conditions or sequence modifications influence peptide structure and assembly behavior. Such investigations provide valuable insight into the physical forces governing amyloid formation. Applications in Alzheimer’s Disease Research and Drug Screening The β-Amyloid (17–24) peptide is widely applied in Alzheimer’s disease research aimed at understanding how amyloid peptides aggregate and interact with other molecules. Because the fragment contains sequence elements essential for aggregation, it provides a useful model for identifying factors that influence fibril formation. In addition to mechanistic studies, the peptide is also used in screening assays designed to identify compounds capable of modulating amyloid aggregation. Researchers can evaluate potential inhibitors or modulators by observing how these molecules affect the aggregation behavior of the peptide. These screening efforts contribute to the development of therapeutic strategies targeting amyloid formation and related pathological processes. Conclusion The β-Amyloid (17–24) peptide represents a central aggregation segment of the amyloid-β sequence that plays a key role in nucleation and fibril formation. Its involvement in structural transitions and intermolecular interactions makes it a valuable model for studying the molecular mechanisms underlying amyloid assembly. Widely used in biophysical, structural, and biochemical studies, this fragment supports research investigating peptide folding, aggregation dynamics, and sequence-specific determinants of amyloid formation. Through these applications, β-Amyloid (17–24) continues to contribute to Alzheimer’s disease research and to efforts aimed at identifying strategies that modulate amyloid aggregation.