The present study addresses the physisorption on gold of two peptides able to mimic the activity respectively of nerve growth factor (NGF) and brain derived neurotrophic factor (BDNF) neurotrophins. NGF(1-14) and BDNF(1-12), both single and binary peptide solutions at the physiological pH, were adsorbed on Au2O3 and the resulting hybrid bionanointerfaces were exposed to Cu(II) ions, known to influence the neurotrophin activity. The cross-interaction energies for peptide molecules in the bulk solution and at the interface with the gold substrate were evaluated by MD calculations. In particular, the physisorption energies of the entangled NGF(1-14)–BDNF(1-12) system were compared with the adsorption energy of each oligopeptide with gold oxide surface. Experimental investigations were carried out by a multitechnique approach based on QCM-D, CD and XPS analyses, to highlight different kinetics/dynamics of peptide-gold interaction, average group orientation as well as peptide coverage of the gold substrate. Comparison of theoretical and experimental results pointed to a significant aggregation of NGF(1-14) and BDNF(1-12) with respect the side on interaction oligopeptide-Au2O3. Finally, the interaction of Cu(II) ions with the different peptide adlayers was found to decrease in the following order: BDNF(1-12), NGF+BDNF, NGF(1-14). Experiments with neuronal cells nicely correlated with the different peptide-functionalization of the gold surfaces.

The competitive and synergic interaction of neurotrophin-derived NGF(1-14) and BDNF(1-12) peptides towards gold oxide surfaces

FORTE, GIUSEPPE;SATRIANO, Cristina;
2013

Abstract

The present study addresses the physisorption on gold of two peptides able to mimic the activity respectively of nerve growth factor (NGF) and brain derived neurotrophic factor (BDNF) neurotrophins. NGF(1-14) and BDNF(1-12), both single and binary peptide solutions at the physiological pH, were adsorbed on Au2O3 and the resulting hybrid bionanointerfaces were exposed to Cu(II) ions, known to influence the neurotrophin activity. The cross-interaction energies for peptide molecules in the bulk solution and at the interface with the gold substrate were evaluated by MD calculations. In particular, the physisorption energies of the entangled NGF(1-14)–BDNF(1-12) system were compared with the adsorption energy of each oligopeptide with gold oxide surface. Experimental investigations were carried out by a multitechnique approach based on QCM-D, CD and XPS analyses, to highlight different kinetics/dynamics of peptide-gold interaction, average group orientation as well as peptide coverage of the gold substrate. Comparison of theoretical and experimental results pointed to a significant aggregation of NGF(1-14) and BDNF(1-12) with respect the side on interaction oligopeptide-Au2O3. Finally, the interaction of Cu(II) ions with the different peptide adlayers was found to decrease in the following order: BDNF(1-12), NGF+BDNF, NGF(1-14). Experiments with neuronal cells nicely correlated with the different peptide-functionalization of the gold surfaces.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/20.500.11769/111937
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