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Spectroscopic characterization and in vitro studies of biological activity of bradykinin derivatives

Eleven multiple analogs of bradykinin—a peptide that is a natural ligand of B1 and B2 receptors but does not bind or activate the B1 receptor unless Arg(9) is removed from the sequence by the action of carboxypeptidase N—were synthesized. Their biological activity was examined on T-REx cell lines ex...

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Detalles Bibliográficos
Autores principales: Proniewicz, Edyta, Burnat, Grzegorz, Domin, Helena, Iłowska, Emilia, Roman, Adam, Prahl, Adam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9643506/
https://www.ncbi.nlm.nih.gov/pubmed/36348016
http://dx.doi.org/10.1038/s41598-022-23448-7
Descripción
Sumario:Eleven multiple analogs of bradykinin—a peptide that is a natural ligand of B1 and B2 receptors but does not bind or activate the B1 receptor unless Arg(9) is removed from the sequence by the action of carboxypeptidase N—were synthesized. Their biological activity was examined on T-REx cell lines expressing B1 or B2 receptors using the intracellular IP1 assay. The mRNA expression of B1R and B2R in the lysate of tumor cell lines, e.g., U87-MG (human astrocytoma), SHP-77 (human small cell lung cancer), and H4 (human brain glioma), was determined. For five B1R antagonists, adsorption at the liquid/solid interface (Au nanoparticles (AuNPs) served as the solid surface) was discussed in terms of the vibrations of molecular fragments (structural factors) responsible for the biological properties of these analogs.