Contact
    Start Publications Tuning the Morphology of Nanostructured Peptide Films by the ...
    ←  Publication Finder
    KSV NIMA

    Tuning the Morphology of Nanostructured Peptide Films by the Introduction of a Secondary Structure Conformational Constraint: A Case Study of Hierarchical Self-Assembly

    Year: 2018

    Journal: J. Phys. Chem. B, Volume 122, JUN 21, page 6305–6313

    Authors: De Zotti, Marta; Muzzi, Beatrice; Gatto, Emanuela; Di Napoli, Benedetta; Mazzuca, Claudia; Palleschi, Antonio; Placidi, Ernesto; Formaggio, Fernando; Toniolo, Claudio; Venanzi, Mariano

    Organizations: European Union's Horizon 2020 Research and Innovation programme under the Marie Sklodowska-Curie [690901]; MIUR [RBFR13RQXM]

    Peptide self-assembly is ubiquitous in nature. It governs the organization of proteins, controlling their folding kinetics and preserving their structural stability and bioactivity. In this connection, model oligopeptides may give important insights into the molecular mechanisms and elementary forces driving the formation of supramolecular structures. In this contribution, we show that a single residue substitution, that is, Aib (alpha-aminoisobutyric acid) in place of Ala at position 4 of an-(L-Ala)(5)-homo-oligomer, strongly alters the aggregation process. In particular, this process is initiated by the formation of small peptide clusters that promote aggregation on the nanometer scale and, through a hierarchical self-assembly, lead to mesoscopic structures of micrometric dimensions. Furthermore, we show that the use of the well-established Langmuir-Blodgett technique represents an effective strategy for coating extended areas of inorganic substrates by densely packed peptide layers, thus paving the way for application of peptide films as templates for biomineralization, biocompatible coating of surfaces, and scaffolds for tissue engineering.
    View publication