Fluorescence study for selecting specific ligands toward HER2 receptor: An example of receptor fragment approach

• Published in: European journal of medicinal chemistry Vol. 61; pp. 116 - 121
• Main Authors: Calce, Enrica, Monfregola, Luca, Sandomenico, Annamaria, Saviano, Michele, De Luca, Stefania
• Format: Journal Article
• Language: English
• Published: PARIS Elsevier Masson SAS 01.03.2013; Elsevier
• Subjects: Antibodies, Monoclonal, Humanized - chemistry; Antibodies, Monoclonal, Humanized - pharmacology; Chemistry, Medicinal; Crystallography, X-Ray; Dose-Response Relationship, Drug; Enzyme Inhibitors - chemical synthesis; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - isolation & purification; Enzyme Inhibitors - pharmacology; Fluorescence; Fluorescence study; Her2 receptor; Humans; Life Sciences & Biomedicine; Ligands; Models, Molecular; Molecular Structure; Peptides - chemical synthesis; Peptides - chemistry; Peptides - isolation & purification; Peptides - pharmacology; Pharmacology & Pharmacy; Receptor fragment model; Receptor, ErbB-2 - antagonists & inhibitors; Receptor, ErbB-2 - chemistry; Receptor, ErbB-2 - metabolism; Science & Technology; Selective ligands; Spectrometry, Fluorescence; Structure-Activity Relationship; Trastuzumab; Fluorescence study; Receptor fragment model; Her2 receptor; Selective ligands; PROTEIN; TRASTUZUMAB; PHAGE DISPLAY; OVARIAN-CANCER; BREAST-CANCER CELLS; COMBINED BIOLOGICAL THERAPY; CARCINOMAS; EXPRESSION; BINDING; ENDOTHELIAL GROWTH-FACTOR

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...