Advanced Optical Materials · 2018 · 34 citations · 24 references
Natural SciencesBiochemistryMaterials ScienceBiophotonicsBiophysical ChemistryNanomaterialsAmyloid FormationFluorescence SpectroscopyPeptide ChemistryProtein-based NanomaterialsQuantum DotsQuantum Dots In BiologyAmyloid NanostructuresBioinspired NanomaterialsCarbon DotsFluorescence Quantum YieldNanoparticle-biomolecule InteractionsOptical AbsorptionProtein FluorescenceSelf-assembling Peptide Nanomaterials
Abstract Nanoscale bioimaging is a highly important scientific and technological tool, where fluorescent (FL) proteins, organic molecular dyes, inorganic quantum dots, and lately carbon dots are widely used as light emitting biolabels. In this work, a new class of visible FL bioorganic nanodots, self‐assembled from short peptides of different composition and origin, is introduced. It is shown that the electronic energy spectrum of native nonfluorescent peptide nanodots (PNDs) is deeply modified upon thermally mediated refolding of their biological secondary structure from native metastable to stable β‐sheet rich structure. This refolding leads to the appearance of a broadband optical absorption across visible region and tunable, excitation‐dependent visible FL of the nanodots with a high quantum yield of ≈30%. It is shown that this intriguing biophotonic effect appears in several peptides/proteins and does not require the presence of aromatic residues. It is assumed that the origin of the phenomenon is related to proton transfer along network of reconstructed intermolecular hydrogen bonds, stabilizing the thermally induced supramolecular β‐sheet structure. The biocompatible FL PNDs can be potentially applied as high‐resolution bioimaging labels toward advanced biotechnology and biomedical theranostics.
24
Semiconductor Clusters, Nanocrystals, and Quantum Dots
A. Paul Alivisatos · Science · 1996 · 11.4K citations
Circular dichroism: Principles and applications
Christopher J. Jones · FEBS Letters · 1995 · 2.5K citations · Full text
Chemical Kinetics and Dynamics
Ilya Prigogine · Annals of the New York Academy of Sciences · 2003 · 912 citations
Natural Sciences, Chemistry, Physics +17
Amyloid fibril formation by an SH3 domain
J. Iñaki Guijarro, Margaret Sunde, Jonathan A. Jones et al. · Proceedings of the National Academy of Sciences · 1998 · 666 citations