Molecular tripods showing fluorescence enhancement upon binding to streptavidin.
We introduce a new approach to biotin-streptavidin assays based on a molecular tripod which consists of biotin, a fluorophore, and a quencher. The interaction between streptavidin and molecular tripods perturbs the ground-state quencher-fluorophore dimeric conformation in the absence of streptavidin and diminishes the intrinsic self-quenching of a quencher-fluorophore pair. The emission intensity of the molecular tripods plus streptavidin is 3.5-5.2 times that of molecular tripods in the absence of streptavidin.
Kim
Tae Woo
TW
Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-747, Korea.
Yoon
Hey Young
HY
Park
Jung-Hyun
JH
Kwon
Oh-Hoon
OH
Jang
Du-Jeon
DJ
Hong
Jong-In
JI
D001710:Biotin / Q000378:metabolism; D005453:Fluorescence; D011485:Protein Binding; D019809:Streptavidin / Q000378:metabolism*
D001710:Biotin; D019809:Streptavidin