Abstract
The work analyzed the chemical and radiochemical stability of the synthesized peptide labeled with a lutetium radioisotope using high-performance liquid chromatography. A fluorescent-labeled peptide, obtained by a solid-phase peptide synthesis, was used to analyze binding to cultures expressing bombesin receptors. The analysis has shown increased chemical and radiochemical stability of the knottin-modified peptide, as compared to the commercial analog, and maintenance of a high ability to bind to receptors on the surface of cancer cells. The structure created on the basis of a short bombesin peptide and knottin possesses increased stability and retains the ability to bind to cancer cells. All this allows us to consider the creation of these structures as a strategy for fabricating stabilizing scaffolds for short peptides for a peptide-receptor therapy.
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