Beta-Amyloid (25-35), HiLyte™ Fluor 488-labeled

Product Name: Beta-Amyloid (25-35), HiLyte™ Fluor 488-labeled

Sequence One Letter Code: HiLyte™ Fluor 488-GSNKGAIIGLM

Sequence Three Letter Code: Hilyte™ Fluor 488-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-OH

Molecular Weight: 1416.7

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C Protected from light

Research Area: Alzheimer's Disease

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Fluorescent dyes

Code Nacres: NA.26

Application: This peptide corresponds to residues 25–35 of β-amyloid and is labeled with HiLyte™ Fluor 488 for fluorescence-based detection. The Aβ(25–35) fragment represents a neurotoxic core region that retains aggregation and cytotoxic properties of full-length β-amyloid. Fluorescent labeling enables real-time monitoring of aggregation, cellular uptake, and intracellular localization. The bright and stable HiLyte™ Fluor 488 signal supports applications in microscopy, binding assays, and kinetic analyses. This peptide is widely used in studies of amyloid toxicity, neurodegeneration mechanisms, and therapeutic screening in Alzheimer’s disease research.

Current Research: Amyloid-β (Aβ) peptides are central to the molecular pathology of Alzheimer’s disease, where their aggregation into oligomers and fibrils contributes to neuronal dysfunction and progressive neurodegeneration. While full-length Aβ peptides such as Aβ(1–40) and Aβ(1–42) are commonly studied, shorter fragments can reproduce many of the structural and toxic properties associated with amyloid aggregation. Among these, the Aβ(25–35) fragment represents a well-characterized neurotoxic core sequence. When labeled with HiLyte™ Fluor 488, this peptide becomes a powerful fluorescent probe that enables visualization and quantitative analysis of amyloid aggregation and cellular interactions. The Aβ(25–35) Region as a Neurotoxic Core The β-amyloid (25–35) sequence lies within the hydrophobic region of the Aβ peptide that contributes significantly to aggregation and cytotoxicity. Despite its relatively short length, this fragment retains many of the functional properties of full-length Aβ peptides, including the ability to self-associate and form β-sheet–rich structures. Because of these properties, the Aβ(25–35) fragment has been widely used as a minimal model of amyloid toxicity. It can induce neuronal stress responses, membrane disruption, and oxidative damage in experimental systems, making it a valuable tool for studying the mechanisms underlying amyloid-induced neurodegeneration. Using a shorter peptide fragment also simplifies experimental analysis, allowing researchers to focus on the key sequence elements responsible for aggregation and toxicity. Fluorescent Labeling with HiLyte™ Fluor 488 To facilitate detection and imaging, the Aβ(25–35) peptide is labeled with HiLyte™ Fluor 488, a green fluorescent dye designed for high brightness and photostability. This fluorophore provides several advantages compared with traditional dyes such as fluorescein (FITC) or FAM. HiLyte Fluor 488 produces strong fluorescence signals with reduced photobleaching, making it well suited for microscopy and long-term imaging experiments. The enhanced signal stability allows researchers to monitor peptide behavior under conditions that might degrade less robust fluorophores. The fluorescent label enables direct visualization of the peptide in biochemical assays and cellular systems, supporting a wide range of fluorescence-based experimental approaches. Monitoring Amyloid Aggregation One of the major applications of the labeled peptide is in amyloid aggregation studies. Fluorescent labeling allows researchers to track peptide assembly in real time as monomers aggregate into oligomers and fibrillar structures. By monitoring changes in fluorescence intensity or distribution, investigators can analyze aggregation kinetics, nucleation events, and fibril growth processes. These experiments provide insight into the molecular mechanisms that drive amyloid assembly and how environmental conditions influence aggregation pathways. Fluorescent peptides also allow aggregation to be visualized directly under microscopy, revealing structural patterns of amyloid formation. Investigating Cellular Uptake and Localization Another important use of the HiLyte Fluor 488–labeled Aβ(25–35) peptide is in cellular uptake experiments. Fluorescent labeling enables researchers to observe how amyloid peptides interact with cell membranes, enter cells, and accumulate within intracellular compartments. These studies help clarify the pathways through which amyloid peptides affect neuronal cells and contribute to toxicity. Visualization of intracellular localization can reveal whether peptides associate with membranes, organelles, or other cellular structures involved in stress responses. Such experiments provide important information about the cellular mechanisms of amyloid-induced damage. Applications in Fluorescence Microscopy The strong fluorescent signal of HiLyte Fluor 488 makes the peptide particularly useful for fluorescence microscopy. Researchers can track the distribution and aggregation of amyloid peptides in cell cultures, tissue samples, or model systems. Microscopy-based experiments allow visualization of amyloid interactions with neuronal membranes, synaptic structures, or intracellular components. These imaging studies help reveal how amyloid aggregates influence cellular architecture and function. Binding Studies and Interaction Analysis Fluorescently labeled peptides can also be used in binding assays to investigate interactions between amyloid peptides and other biomolecules. Researchers may examine how proteins, antibodies, or small molecules bind to amyloid sequences and influence aggregation behavior. Such experiments are particularly valuable for identifying molecules that modulate amyloid assembly or inhibit toxic interactions with cellular membranes. Kinetic and Mechanistic Investigations Because fluorescence signals can be measured quantitatively, the labeled peptide is well suited for kinetic analyses of amyloid formation. Researchers can measure rates of peptide aggregation and determine how factors such as temperature, ionic strength, or binding partners influence amyloid assembly. These kinetic studies provide deeper insight into the molecular mechanisms that control amyloid formation and stability. Relevance to Alzheimer’s Disease Research Understanding how amyloid peptides aggregate and exert toxic effects on neurons is essential for uncovering the molecular basis of Alzheimer’s disease. Fluorescent tools such as the HiLyte Fluor 488–labeled Aβ(25–35) peptide allow researchers to visualize and quantify these processes in detail. The peptide is widely used in neurodegeneration research, where it supports studies of amyloid toxicity, cellular stress pathways, and interactions between amyloid aggregates and neuronal membranes. Conclusion The HiLyte™ Fluor 488–labeled β-amyloid (25–35) peptide combines a well-established neurotoxic amyloid fragment with a bright and photostable fluorescent probe. This combination enables sensitive detection and visualization of amyloid aggregation, cellular uptake, and peptide interactions. Through applications in fluorescence microscopy, aggregation assays, binding studies, and kinetic analyses, the peptide serves as a valuable tool for investigating amyloid assembly and the mechanisms underlying amyloid-associated neurodegeneration in Alzheimer’s disease research.