Fluorescence resonance energy transfer in a novel cyclodextrin-peptide conjugate for detecting steroid molecules.
A novel cyclodextrin conjugated peptide, 1, having two different fluorophores, coumarin and pyrene, in the side chains has been designed and synthesized. The circular dichroism study reveals that 1 shows typical alpha-helix pattern, and forms intramolecular inclusion complex with coumarin. The fluorescence emission study shows that the peptide exhibits intramolecular fluorescence resonance energy transfer (FRET) without quenching of two fluorophores. We have determined the binding constants of 1 for various biologically important steroid molecules as guests using the guest-responsive variation in the fluorescence emission intensity of coumarin.
Hossain
Mohammed Akhter
MA
Department of Bioengineering, Tokyo Institute of Technology, 4259Nagatsuta, Midori, Yokohama 226-8501, Japan.
Mihara
Hisakazu
H
Ueno
Akihiko
A
D002942:Circular Dichroism; D003505:Cyclodextrins / Q000138:chemical synthesis* / Q000737:chemistry; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D007202:Indicators and Reagents; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D011487:Protein Conformation; D013256:Steroids / Q000032:analysis*
D003505:Cyclodextrins; D007202:Indicators and Reagents; D010455:Peptides; D013256:Steroids