Shepherdin (79-87) is amino acids 79 to 87 fragment of Shepherdin. Shepherdin is a peptidomimetic antagonist of the complex between Hsp90 and Survivin. Anticancer activity.
CAT No: R1675
CAS No:861224-28-4
Synonyms/Alias:shepherdin;861224-28-4;Shepherdin 79-87;(2S)-2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2,6-diaminohexanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]-3-sulfanylpropanoyl]amino]propanoyl]amino]-3-phenylpropanoyl]amino]-3,3-dimethylbutanoic acid;NSC-741765;DTXSID10661626;NSC741765;DA-57832;L-Lysyl-L-histidyl-L-seryl-L-serylglycyl-L-cysteinyl-L-alanyl-L-phenylalanyl-3-methyl-L-valine;
Shepherdin 79-87 is a synthetic peptide fragment derived from the larger Shepherdin sequence, designed to mimic a specific region of the heat shock protein 90 (Hsp90) binding motif. As a research peptide, it is notable for its role in modulating protein-protein interactions within the cellular chaperone machinery, particularly those associated with molecular folding, stability, and cell survival pathways. Due to its defined amino acid sequence and targeted biochemical activity, Shepherdin 79-87 has become a valuable tool for probing the mechanistic underpinnings of chaperone-dependent signaling networks and for exploring the structural-functional relationships of peptide-based modulators in cellular systems.
Protein-Protein Interaction Studies: In the context of molecular chaperone research, Shepherdin 79-87 is widely utilized to investigate the dynamics of Hsp90-client protein complexes. Its sequence specificity enables researchers to dissect the contributions of individual binding motifs to the overall stability and function of multi-protein assemblies. By acting as a competitive inhibitor or molecular probe, the peptide facilitates detailed mapping of interaction domains, offering insights into the regulation of chaperone-mediated protein folding and stabilization processes. This application is particularly valuable for elucidating the molecular basis of cellular stress responses and proteostasis.
Peptide-Protein Binding Assays: The defined structure of Shepherdin 79-87 makes it an ideal candidate for in vitro and in vivo binding assays aimed at quantifying the affinity and specificity of peptide-mediated interactions with Hsp90 and related chaperones. Researchers employ the peptide in surface plasmon resonance, fluorescence polarization, or co-immunoprecipitation experiments to characterize binding kinetics, identify critical contact residues, and validate the functional relevance of peptide-chaperone associations. Such assays are instrumental in advancing the understanding of allosteric regulation and the design of novel peptide-based modulators.
Cellular Pathway Modulation: By introducing Shepherdin 79-87 into cultured cells, investigators can selectively perturb chaperone-dependent signaling cascades, enabling the study of downstream effects on cellular proliferation, apoptosis, and stress adaptation mechanisms. The peptide serves as a functional tool for dissecting the role of Hsp90 in maintaining cellular homeostasis, supporting experiments that aim to delineate the molecular checkpoints governing cell fate decisions. These studies contribute to a broader comprehension of cellular quality control systems and their regulation by exogenous peptides.
Peptide Structure-Activity Relationship (SAR) Analysis: The modular nature of Shepherdin 79-87 allows for systematic modifications and analog development to assess the impact of sequence alterations on biological activity. Researchers use the peptide as a template for SAR studies, synthesizing derivatives with targeted substitutions or modifications to probe structure-function relationships. Such investigations are essential for optimizing peptide stability, binding affinity, and functional efficacy, thereby informing the rational design of next-generation research peptides with enhanced properties.
Peptide Delivery and Uptake Studies: Due to its manageable size and well-characterized sequence, Shepherdin 79-87 is frequently employed in experiments evaluating cellular uptake, intracellular localization, and delivery strategies for bioactive peptides. Researchers leverage its properties to test various delivery vehicles, such as nanoparticles, liposomes, or cell-penetrating motifs, assessing their effectiveness in facilitating peptide entry and distribution within biological systems. These studies are critical for advancing peptide-based research tools and for developing methodologies that improve the intracellular targeting of functional biomolecules.
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