Development of protein surface recognition probe: Selective fluorescent sensing of monophosphorylated peptide.
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Accession number;04A0258611
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| Title;Development of protein surface recognition probe: Selective fluorescent sensing of monophosphorylated peptide. |
| Author;
OJIDA AKIO
(Kyushu Univ., Graduate School, JPN)
INOUE MASAAKI
(Kyushu Univ., Graduate School, JPN)
MITOOKA YASUKO
(Kyushu Univ., Graduate School, JPN)
HAMACHI ITARU
(Kyushu Univ., Graduate School, JPN)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.18th;NO.;PAGE.56-57(2003)
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| Figure&Table&Reference;FIG.4, REF.1 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;We report novel fluorescent chemosensors toward a phosphorylated peptide surface. Anthracene derivatives having two sets of zinc(II)-dipicolylamine 1 and 2 selectively bind phosphorylated chemical species and intensified their fluorescence intensity due to the anthracene moiety. On the basis of 1H-NMR, 31P-NMR, and a single crystal X-ray analysis, we revealed that two Zn(II)-Dpa units of the receptors cooperatively act to bind the phosphate sites of these derivatives. These chemosensors show sequence selective affinities toward a variety of phosphorylated peptides and can sense a phosphorylated with the high affinity (-107 M-1) in aqueous solution. Good agreement of the binding affinity estimated by isothermal titration calorimetry (ITC) with fluorescence titration indicated that the fluorescence change of the receptors directly reflects the biding to the phospohrylated peptides. Furthermore, the detailed titration experiments clarified that the phosphate anion-assisted coordination of the second Zn(II) to the binuclear receptors is crucial for the fluorescence intensification upon binding to the phosphorylated derivatives. (author abst.) |
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