title: Modification of fluorophore photophysics through peptide-driven self-assembly.
abstract: We describe the formation of self-assembling nanoscale fibrillar aggregates from a hybrid system comprising a short polypeptide conjugated to the fluorophore fluorene. The fibrils are typically unbranched, approximately 7 nm in diameter, and many microns in length. A range of techniques are used to demonstrate that the spectroscopic nature of the fluorophore is significantly altered in the fibrillar environment. Time-resolved fluorescence spectroscopy reveals changes in the guest fluorophore, consistent with energy migration and excimer formation within the fibrils. We thus demonstrate the use of self-assembling peptides to drive the assembly of a guest moiety, in which novel characteristics are observed as a consequence. We suggest that this method could be used to drive the assembly of a wide range of guests, offering the development of a variety of useful, smart nanomaterials that are able to self-assemble in a controllable and robust fashion.
authors: Cavendish Laboratory, University of Cambridge, JJ Thomson Avenue, Cambridge, UK.
authors: Kevin J
authors: KJ
authors: Channon
authors: Glyn L
authors: GL
authors: Devlin
authors: Steven W
authors: SW
authors: Magennis
authors: Chris E
authors: CE
authors: Finlayson
authors: Anna K
authors: AK
authors: Tickler
authors: Carlos
authors: C
authors: Silva
authors: Cait E
authors: CE
authors: MacPhee
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry*; D005449:Fluorenes / Q000737:chemistry*; D005456:Fluorescent Dyes / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D000682:Amyloid; D005449:Fluorenes; D005456:Fluorescent Dyes; D010455:Peptides; C041509:fluorene