Cy5-Amyloid β Peptide (42-1) (human) features a Cy5 fluorophore conjugated to the Aβ(42-1) sequence, enabling visualization of aggregation and binding events. The peptide preserves the hydrophobic and β-structure-forming motifs of the parent Aβ region. Researchers track fibrillization kinetics and interactions with membranes or chaperones using fluorescence methods. Applications include aggregation-mechanism studies, inhibitor screening, and supramolecular-assembly research.
CAT No: Z10-101-191
Cy5-Amyloid β Peptide (42-1)(human) is a synthetic peptide derivative that combines the reversed sequence of the human amyloid beta (Aβ) 1-42 peptide with a covalently attached Cy5 fluorescent dye. This compound is designed to facilitate advanced studies of amyloid aggregation, protein misfolding, and neurodegenerative disease mechanisms by providing a robust fluorescent signal for sensitive detection. Its reversed sequence offers a valuable negative control for comparative studies, allowing researchers to distinguish sequence-specific effects from nonspecific interactions. As a versatile biochemical tool, Cy5-Amyloid β Peptide (42-1)(human) supports a wide range of fluorescence-based assays and imaging applications in neurobiology and protein aggregation research.
Fluorescence imaging: The Cy5 label enables direct visualization of peptide localization and distribution in various biological matrices. Researchers commonly employ this fluorescent peptide in confocal microscopy, flow cytometry, and live-cell imaging to track peptide uptake, intracellular trafficking, or extracellular deposition. The strong far-red emission of Cy5 minimizes background autofluorescence and spectral overlap, enhancing signal-to-noise ratios in complex biological samples. This makes the compound particularly useful for studying peptide behavior in cultured neurons, brain tissue slices, or in vitro aggregation models.
Protein aggregation studies: As a reversed-sequence analog of Aβ(1-42), the peptide serves as a critical negative control in amyloid aggregation assays. Its sequence inversion disrupts the native aggregation propensity of the wild-type peptide, allowing researchers to differentiate specific amyloidogenic mechanisms from nonspecific aggregation or dye-related artifacts. By including this control in thioflavin T fluorescence assays, transmission electron microscopy, or dynamic light scattering experiments, investigators can validate the sequence dependence of aggregation phenomena and refine their understanding of amyloid formation pathways.
Assay development and validation: The unique combination of a reversed amyloid sequence and a Cy5 fluorophore makes this peptide an essential tool for optimizing and validating high-throughput screening assays targeting amyloid-beta interactions. It provides a reference for assessing assay specificity, sensitivity, and dynamic range, particularly in fluorescence polarization, FRET, or time-resolved fluorescence formats. By benchmarking assay performance with this control peptide, developers can minimize false positives and ensure robust detection of sequence-specific binding events or modulatory effects.
Biophysical interaction analysis: The compound is widely utilized in studies investigating the molecular interactions between amyloid peptides and small molecules, proteins, or cellular components. Its fluorescent tag allows for real-time monitoring of binding kinetics, affinity measurements, and competitive displacement assays using techniques such as surface plasmon resonance or fluorescence anisotropy. The reversed sequence ensures that observed interactions are attributable to specific structural features of the native peptide, rather than generic peptide properties or dye effects.
Neurodegeneration model controls: In neurobiology research, the reversed-sequence Cy5-labeled peptide is frequently used as a control to evaluate the specificity of cellular responses to amyloid-beta exposure. By comparing the effects of wild-type and reversed peptides on neuronal viability, synaptic function, or cellular signaling, scientists can distinguish between sequence-dependent toxicity and nonspecific stress responses. This approach is instrumental in refining experimental models of Alzheimer's disease and related neurodegenerative disorders, supporting the development of targeted interventions and mechanistic insights.
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