Psma I&S provides a structured peptide-based system commonly used to investigate targeting motifs and ligand orientation. Its design supports analyses of binding affinity, conformational adaptability, and sequence-derived specificity. Researchers explore its behavior in modeling surface interactions and receptor-recognition patterns. Broader applications span molecular imaging probe design, peptide chemistry, and affinity optimization.
CAT No: R2445
CAS No:2639475-07-1
Synonyms/Alias:PSMA I&S;2639475-07-1;EX-A8579;HY-148152;CS-0613795;(2S)-2-[[(1S)-1-carboxy-5-[[8-[[(5R)-5-carboxy-5-[[(2R)-2-[[(2R)-2-[[(2R)-3-hydroxy-2-[[(2R)-3-hydroxy-2-[[(2R)-3-hydroxy-2-[(2-sulfanylacetyl)amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-naphthalen-2-ylpropanoyl]amino]pentyl]amino]-8-oxooctanoyl]amino]pentyl]carbamoylamino]pentanedioic acid;
Psma I&S is a specialized peptide compound designed to target the prostate-specific membrane antigen (PSMA), a cell surface protein highly expressed in prostate cancer and certain other malignancies. As a synthetic peptide, it possesses a defined amino acid sequence that enables selective binding to PSMA, making it a valuable research tool in the field of oncology, molecular imaging, and targeted delivery. The compound's biochemical specificity and affinity for PSMA underlie its significance in studies aimed at understanding tumor biology, developing targeted diagnostic strategies, and exploring innovative therapeutic approaches in preclinical settings.
Target validation: In oncology research, PSMA-targeting peptides such as Psma I&S are employed to validate PSMA as a biomarker and therapeutic target. By enabling selective recognition of PSMA-expressing cells, the compound facilitates studies that elucidate the distribution, density, and role of PSMA in tumor progression. Researchers utilize it to confirm target engagement and to assess the relevance of PSMA expression in various cancer models, providing a foundation for the rational design of targeted interventions.
Molecular imaging probe development: The specific binding characteristics of this peptide make it ideal for the development of molecular imaging probes. By conjugating imaging moieties such as fluorescent dyes or radiolabels to the peptide, investigators can create targeted agents for visualizing PSMA-positive tumors in animal models. This application supports the advancement of non-invasive imaging techniques, enabling real-time monitoring of tumor localization, disease progression, and response to experimental therapies.
Drug delivery research: The high affinity and selectivity of PSMA-binding peptides are leveraged in the design of targeted drug delivery systems. Researchers can conjugate cytotoxic agents, nanoparticles, or other therapeutic cargos to the peptide, directing their accumulation to PSMA-expressing tumor cells. This strategy enhances the specificity of drug delivery in preclinical models, potentially reducing off-target effects and improving the efficacy of investigational compounds in laboratory studies.
Binding affinity and structure-activity relationship studies: Psma I&S is frequently utilized in biochemical assays to characterize the binding kinetics and structure-activity relationships of PSMA ligands. By systematically modifying the peptide sequence or functional groups, researchers can assess the impact on binding affinity, specificity, and stability. These insights are critical for optimizing ligand design, informing the development of more effective PSMA-targeted agents for research applications.
Competitive inhibition and receptor occupancy assays: The peptide serves as a valuable competitor in assays designed to evaluate the binding of other PSMA-targeting molecules. By acting as a reference ligand, it enables quantification of receptor occupancy, competitive inhibition, and displacement kinetics in cell-based or biochemical systems. Such studies are essential for benchmarking new PSMA-targeted compounds, understanding their mechanism of action, and guiding the selection of lead candidates for further research and development.
1. Implications of ligand-receptor binding kinetics on GLP-1R signalling
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