Novel peptides bearing pyrene and coumarin units with or without beta-cyclodextrin in their side chains exhibit intramolecular fluorescence resonance energy transfer.
Novel peptides bearing the pyrene/coumarin FRET pair in their side chains have been designed and synthesized. Peptide 1 having endogenous beta-cyclodextrin (beta-CD) in the side chain exhibits FRET in aqueous solution, indicating that coumarin, being accommodated into the CD cavity, is separated from pyrene. Guest-induced quenching of the fluorophores in 1 indicates that coumarin, being excluded from the CD cavity, comes into close contact with pyrene. Peptide 2 shows FRET only after addition of external beta-CD that again reflects the idea that beta-CD surely caps the coumarin unit in its hydrophobic cavity, and, therefore, quenching of the fluorophores can be prevented in FRET peptide probes. With this strategy, various peptide-based FRET probes can be developed that would be useful for studying biological phenomena in living cells.
Hossain
Mohammed Akhter
MA
Department of Bioengineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori, Yokohama 226-8501, Japan.
Mihara
Hisakazu
H
Ueno
Akihiko
A
D002942:Circular Dichroism; D003374:Coumarins / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer; D010455:Peptides / Q000737:chemistry*; D011721:Pyrenes / Q000737:chemistry*; D047392:beta-Cyclodextrins / Q000032:analysis / Q000737:chemistry*
D003374:Coumarins; D010455:Peptides; D011721:Pyrenes; D047392:beta-Cyclodextrins; C030123:coumarin; C031215:betadex