Solvent-Free procedure of an A9 Peptide Dimer Exhibiting Specific HER2 Receptor Binding: Fluorescence Spectroscopy Evaluation of the Enhanced Binding Affinity
HER2-expressing cancers currently benefit from targeted therapies, including monoclonal antibodies and antibody-drug conjugates that specifically bind to the extracellular domain of the receptor. Peptides targeting HER2 represent promising candidates for the development of alternative molecular drugs. In this study, we report a dimeric version of the previously validated A9 peptide as a ligand specifically targeting HER2. The novel A9-PEG-A9 conjugate consists of two A9 peptides whose N-terminal amino groups are linked via a polyethylene glycol chain. It was synthesized using a solvent-free protocol and validated as an improved ligand, demonstrating enhanced water solubility and increased affinity for the model receptor HER2-DIVMP, as determined by the fluorescence spectroscopy titration method.
Authors
- Stefania De Luca (ORCID: https://orcid.org/0000-0002-7078-1696)
- Emanuela Iaccarino (ORCID: https://orcid.org/0000-0002-9073-0204)
- Valentina Verdoliva (ORCID: https://orcid.org/0000-0003-4689-7856)
- Giuseppe Digilio (ORCID: https://orcid.org/0000-0003-2397-2913)
Institutions
- Università degli Studi del Piemonte Orientale “Amedeo Avogadro” (IT)
- Institute of Biostructure and Bioimaging (IT)
- National Research Council (IT)
- Institute of Crystallography (IT)
Publication Details
- Journal
- Journal of Medicinal Chemistry
- Published
- 2025-07-24
- DOI
- https://doi.org/10.1021/acs.jmedchem.5c01194
- Citations
- 1
- Primary Topic
- Monoclonal and Polyclonal Antibodies Research
- Type
- article
- Field-Weighted Citation Impact
- 1.36
Funders
- Ministero dell'Università e della Ricerca