Article ID | Journal | Published Year | Pages | File Type |
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1394370 | European Journal of Medicinal Chemistry | 2013 | 6 Pages |
Fluorescence titrations allowed us to study the interaction process between Herceptin (Fab)-derived peptides and a synthetic peptide mimicking a subdomain IV of the receptor HER2 (HER2-DIVMP). For some of the investigated peptide/HER2-DIVMP complexes a nanomolar dissociation constant was found. The performed interaction studies were completely immune from interferences of other receptor domains not covered by the design, thus decreasing the possibilities of selecting potential ligands able to bind other subtypes of HER2 receptor family. Our results demonstrate that the adopted receptor fragment approach represents an efficient methodology for selecting new molecules as lead structures specific for the receptor target. For these reasons the optimized compounds could be employed as delivery agents for the receptor-mediated anticancer therapy.
Graphical abstractFluorescence studies allowed the selection of ligands highly specific for domain IV of HER2 receptor. This methodology, which used the receptor fragment approach, proved to be a reliable screening technique.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Receptor fragment approach was adopted. ► Peptide ligands selected for HER2 domain IV were developed. ► Fluorescence spectroscopy revealed to be fast and sensitive technique.