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.

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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

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article

Solvent-Free procedure of an A9 Peptide Dimer Exhibiting Specific HER2 Receptor Binding: Fluorescence Spectroscopy Evaluation of the Enhanced Binding Affinity

Stefania De Luca, Emanuela Iaccarino, Valentina Verdoliva, Giuseppe Digilio
1 citations
Journal of Medicinal Chemistry
Monoclonal and Polyclonal Antibodies Research
1.36
article

Solvent-Free procedure of an A9 Peptide Dimer Exhibiting Specific HER2 Receptor Binding: Fluorescence Spectroscopy Evaluation of the Enhanced Binding Affinity

Stefania De Luca, Emanuela Iaccarino, Valentina Verdoliva, Giuseppe Digilio
article en
1 citations

Abstract

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.

Journal of Medicinal ChemistryVol. 68(15)
Università degli Studi del Piemonte Orientale “Amedeo Avogadro” (IT), Institute of Biostructure and Bioimaging (IT), National Research Council (IT), Institute of Crystallography (IT)
Ministero dell'Università e della Ricerca
Openalex Percentile: Top 18%
Monoclonal and Polyclonal Antibodies Research
1.36
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Solvent-Free procedure of an A9 Peptide Dimer Exhibiting Specific HER2 Receptor Binding: Fluorescence Spectroscopy Evaluation of the Enhanced Binding Affinity — Stefania De Luca, Emanuela Iaccarino, et al. · Journal of Medicinal Chemistry (2025) | TGRS Research Map | TGRS