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.

Tuning the Morphology of Nanostructured Peptide Films by the Introduction of a Secondary Structure Conformational Constraint: A Case Study of Hierarchical Self-Assembly / De Zotti, M.; Muzzi, B.; Gatto, E.; Di Napoli, B.; Mazzuca, C.; Palleschi, A.; Placidi, E.; Formaggio, F.; Toniolo, C.; Venanzi, M.. - In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL. - ISSN 1520-6106. - 122:24(2018), pp. 6305-6313. [10.1021/acs.jpcb.8b01877]

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

Placidi E.;
2018

Abstract

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.
2018
Air; Aminoisobutyric Acids; Microscopy, Atomic Force; Molecular Dynamics Simulation; Nanostructures; Oligopeptides; Protein Structure, Secondary; Spectrometry, Fluorescence; Water
01 Pubblicazione su rivista::01a Articolo in rivista
Tuning the Morphology of Nanostructured Peptide Films by the Introduction of a Secondary Structure Conformational Constraint: A Case Study of Hierarchical Self-Assembly / De Zotti, M.; Muzzi, B.; Gatto, E.; Di Napoli, B.; Mazzuca, C.; Palleschi, A.; Placidi, E.; Formaggio, F.; Toniolo, C.; Venanzi, M.. - In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL. - ISSN 1520-6106. - 122:24(2018), pp. 6305-6313. [10.1021/acs.jpcb.8b01877]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1325899
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