Hsp70-derived octapeptide is a conserved octapeptide of the C-terminal end of Hsp70, which physically interacts with tetratricopeptide repeat (TPR) motifs.
CAT No: R1433
CAS No:736171-62-3
Synonyms/Alias:Hsp70-derived octapeptide;736171-62-3;HY-P1896;DA-54107;MS-31589;CS-0097986;G16859;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S,3R)-2-[[(2S)-1-(2-aminoacetyl)pyrrolidine-2-carbonyl]amino]-3-hydroxybutanoyl]amino]-3-methylpentanoyl]amino]-4-carboxybutanoyl]amino]-4-carboxybutanoyl]amino]-3-methylbutanoyl]amino]butanedioic acid;
Hsp70-derived octapeptide is a synthetic peptide fragment originating from the highly conserved heat shock protein 70 (Hsp70) family. As a short peptide sequence derived from a key molecular chaperone, it retains specific structural motifs that are critical for protein-protein interactions and cellular stress response pathways. Its biochemical relevance lies in its capacity to mimic or modulate certain functional aspects of the parent protein, making it a valuable molecular tool for dissecting the mechanisms underlying protein homeostasis, cellular signaling, and chaperone-mediated processes. The octapeptide format offers a manageable and well-defined system for probing sequence-specific effects in various experimental settings, supporting advanced research in molecular biology, biochemistry, and cell physiology.
Protein interaction studies: Researchers frequently employ the Hsp70-derived octapeptide to investigate the molecular determinants of Hsp70-client protein interactions. The peptide serves as a minimal binding motif, enabling precise mapping of chaperone recognition sites and elucidating the sequence elements responsible for substrate affinity. By introducing this peptide into in vitro or cell-based assays, scientists can dissect the competitive dynamics of chaperone-substrate complexes, providing critical insight into the selectivity and regulation of protein folding machinery.
Chaperone pathway modulation: The octapeptide is utilized in studies aiming to modulate chaperone activity, either by acting as a competitive inhibitor or as a probe for allosteric regulation. Its defined sequence allows for targeted disruption or enhancement of Hsp70-associated pathways, facilitating the analysis of downstream effects on protein aggregation, degradation, or trafficking. Such applications are instrumental in unraveling the cellular consequences of altered chaperone function and in identifying potential nodes of regulation within the proteostasis network.
Cellular stress response research: As a molecular mimic of a key Hsp70 epitope, the peptide is valuable in exploring the cellular stress response. By introducing the octapeptide into experimental systems, investigators can assess its impact on the induction or attenuation of heat shock response elements, stress granule formation, and adaptive signaling cascades. These studies contribute to a deeper understanding of how cells sense and respond to proteotoxic stress, with the octapeptide serving as a controllable tool for modulating these pathways in a reproducible manner.
Peptide structure-function analysis: The Hsp70-derived octapeptide provides a well-defined platform for systematic structure-activity relationship studies. Researchers can apply mutational analysis or chemical modification to this sequence, evaluating the impact of specific residues on biological activity, stability, or binding affinity. Such investigations are fundamental for delineating the structural features that govern peptide function, informing the rational design of peptide-based modulators or probes.
Peptide-based assay development: The defined nature and biological relevance of the octapeptide make it a useful component in the development of high-throughput screening assays and biosensors. By incorporating the peptide into binding or activity assays, scientists can establish sensitive and specific platforms for monitoring chaperone interactions, inhibitor screening, or detection of molecular partners. These assay systems facilitate robust and reproducible measurement of chaperone-related activities, supporting both basic research and early-stage drug discovery efforts.
1. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
2. The spatiotemporal control of signalling and trafficking of the GLP-1R
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