Engineered β-hairpin scaffolds from human prion protein regions: Structural and functional investigations of aggregates(178 views) Di Natale C, La Manna S, Avitabile C, Florio D, Morelli G, Netti PA, Marasco D
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 4.831, 5-year impact factor: 3.39
Url: Not available.
Keywords: Amyloid Fiber, Confocal Microscopy, Prion Peptide, Second Harmonic Generation,
Affiliations: *** IBB - CNR ***
Department of Pharmacy, CIRPEB: Centro Interuniversitario di Ricerca sui Peptidi Bioattivi- University of Naples "Federico II", Via Mezzocannone 16, 80134 Naples, Italy
Center for Advanced Biomaterials for Healthcare@CRIB, Istituto Italiano di Tecnologia (IIT), Largo Barsanti e Matteucci 53, 80125 Naples, Italy.
Institute of Biostructures and Bioimaging (IBB), National Research Council, Via Mezzocannone 16, 80134 Naples, Italy.
Task force di Ateneo"METODOLOGIE ANALITICHE PER LA SALVAGUARDIA DEI BENI CULTURALI" MASBC, University of Naples "Federico II", Italy. Electronic address: daniela.marasco@unina.it.
References: Not available.
Engineered β-hairpin scaffolds from human prion protein regions: Structural and functional investigations of aggregates
The investigation of conformational features of regions of amyloidogenic proteins are of great interest to deepen the structural changes and consequent self-aggregation mechanisms at the basis of many neurodegenerative diseases. Here we explore the effect of β-hairpin inducing motifs on regions of prion protein covering strands S1 and S2. In detail, we unveiled the structural and functional features of two model chimeric peptides in which natural sequences are covalently linked together by two dipeptides (l-Pro-Gly and d-Pro-Gly) that are known to differently enhance β-hairpin conformations but both containing N- and the C-terminal aromatic cap motifs to further improve interactions between natural strands. Spectroscopic investigations at solution state indicate that primary assemblies of the monomers of both constructs follow different aggregativemechanisms during the self-assembly: these distinctions, evidenced by CD and ThT emission spectroscopies, reflect into great morphological differences of nanostructures and suggest that rigid β-hairpin conformations greatly limit amyloid-like fibrillogenesis. Overall data confirm the important role exerted by the β-structure of regions S1 and S2 during the aggregation process and lead to speculate to its persistence even in unfolding conditions.
Engineered β-hairpin scaffolds from human prion protein regions: Structural and functional investigations of aggregates
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Engineered β-hairpin scaffolds from human prion protein regions: Structural and functional investigations of aggregates