Amyloid β Peptide (42-1)(human) is the inactive form of Amyloid β Peptide (1-42). Amyloid β Peptide (42-1) is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.
CAT No: R1191
CAS No:317366-82-8
Synonyms/Alias:317366-82-8;Amyloid beta Peptide (42-1)(human);|A-Amyloid (42-1), human;AKOS024457599;CID 90488838;PD079487;S-317366-82-8;
Amyloid β Peptide (42-1)(human) is a synthetic peptide corresponding to the reverse sequence of the 42-amino acid amyloid beta (Aβ) peptide found in human tissues. As a reverse-sequence analog of the well-studied Aβ(1-42) fragment, it is inherently resistant to the aggregation and fibrillization properties characteristic of native amyloid beta peptides. This unique structural orientation makes it a valuable tool in biochemical research focused on neurodegenerative disease mechanisms, protein aggregation, and peptide interaction studies. Its utility is grounded in its ability to serve as a negative control or reference standard for investigations into amyloidogenic processes, enabling researchers to distinguish sequence-specific effects from nonspecific peptide phenomena.
Negative Control in Aggregation Studies: The reverse-sequence configuration of Amyloid β Peptide (42-1)(human) makes it an ideal negative control in amyloid aggregation assays. Unlike the native Aβ(1-42), which readily forms oligomers and fibrils associated with neurodegenerative pathologies, the reverse peptide does not exhibit the same propensity for self-assembly. Researchers use it to validate the specificity of aggregation assays and to discriminate between sequence-driven aggregation and nonspecific peptide interactions. This application is critical for ensuring experimental rigor and for interpreting the biological relevance of aggregation phenomena in vitro.
Mechanistic Investigations of Amyloidogenesis: In mechanistic studies of amyloid formation, the reverse-sequence peptide provides a valuable comparative model. By contrasting the behavior of Aβ(42-1) with that of native or mutant amyloid beta peptides, investigators can elucidate the structural determinants and sequence motifs responsible for aggregation, toxicity, or peptide-protein interactions. Such comparative analyses contribute to a deeper molecular understanding of amyloidogenic pathways, supporting the development of new hypotheses and experimental models in neurodegenerative disease research.
Peptide-Protein Interaction Studies: The use of reverse-sequence Aβ allows for the examination of sequence specificity in peptide-protein binding interactions. By assessing binding affinities and interaction profiles in the presence of Aβ(42-1), researchers can identify non-specific interactions that may otherwise confound studies using the native peptide. This approach is particularly valuable in high-throughput screening platforms, where distinguishing true biological targets from artifacts is essential for the discovery of modulators or inhibitors relevant to amyloid biology.
Analytical Method Development and Validation: The unique properties of Amyloid β Peptide (42-1)(human) make it a suitable standard in the development and validation of analytical methods, such as mass spectrometry, chromatography, or immunoassays targeting amyloid peptides. Its resistance to aggregation and distinct sequence orientation provide a benchmark for assessing assay specificity, sensitivity, and reproducibility. Analytical laboratories can employ the peptide to optimize detection protocols and to verify the absence of cross-reactivity or false positives in amyloid quantification workflows.
Structural and Biophysical Characterization: Structural biology and biophysical research benefit from the inclusion of the reverse-sequence peptide as a reference or control. Studies employing techniques such as circular dichroism spectroscopy, nuclear magnetic resonance, or electron microscopy use Aβ(42-1) to contrast folding, secondary structure, and assembly properties with those of amyloidogenic peptides. These comparative analyses yield insights into the conformational dynamics and physicochemical parameters that govern peptide behavior, advancing the broader understanding of protein misfolding and aggregation phenomena.
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