Modification of fluorophore photophysics through peptide-driven self-assembly.
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.
Channon
Kevin J
KJ
Cavendish Laboratory, University of Cambridge, JJ Thomson Avenue, Cambridge, UK.
Devlin
Glyn L
GL
Magennis
Steven W
SW
Finlayson
Chris E
CE
Tickler
Anna K
AK
Silva
Carlos
C
MacPhee
Cait E
CE
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
D000682:Amyloid; D005449:Fluorenes; D005456:Fluorescent Dyes; D010455:Peptides; C041509:fluorene