The importance of being Aib. Aggregation and self‐assembly studies on conformationally constrained oligopeptides. (5th January 2017)

• Record Type: Journal Article
• Authors: Venanzi, Mariano; Gatto, Emanuela; Formaggio, Fernando; Toniolo, Claudio
• Other Names: Alemán Carlos guestEditor.; Hamley Ian W. guestEditor.; Reches Meital guestEditor.
• Is Part Of: Journal of peptide science. Volume 23:Number 2(2017)
• Page Start: 104
• Page End: 116
• Publication Date: 2017-01-05
• Subjects: α‐aminoisobutyric acid -- conformationally constrained α‐amino acid -- peptide aggregation -- peptide fibers -- peptide self‐assembled monolayers; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2956
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : The role of the conformationally constrained α ‐aminoisobutyric acid (Aib) residue in the aggregation and self‐assembly properties of oligopeptides is discussed, critically reviewing our recent work in the field. In this connection, three significant case studies are presented: (i) aggregation propensity of Aib homo‐oligopeptides of different length; (ii) perturbation of the conformational and aggregation properties of Ala‐based pentapeptides by a single Aib versus Ala substitution; and (iii) build up of self‐assembled monolayers formed by Aib homo‐hexapeptide building blocks. The peptides investigated were all functionalized by a fluorescent probe, that is, a naphthyl group in the first case‐study and a pyrenyl group in the other two, with the aim at applying optical spectroscopy techniques and evaluating the relevance of aromatic interactions in the aggregation process. Microscopy techniques at nanometric resolution and results of molecular dynamics simulations are also presented to analyze how the conformational properties of the peptide building blocks would affect the morphology of the peptide aggregates from the nanoscale to the mesoscale. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd. Abstract : The role of the conformationally constrained α ‐aminoisobutyric acid (Aib) residue is discussed in three significant case‐studies illustrating the following: The aggregation propensity of Aib homo‐oligopeptides of different lenght; the perturbation of the conformational and aggregation properties of Ala‐based pentapeptides by a single Aib versus Ala substitution; the build up of self‐assembled monolayers formed by Aib homo‐hexapeptide building blocks.