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Receptor-based fluorescent sensors constructed from ribonucleopeptide.
Nakano, Shun; Konishi, Hiroaki; Morii, Takashi.
Afiliación
  • Nakano S; Institute of Advanced Energy, Kyoto University, Uji, Kyoto, Japan.
  • Konishi H; Institute of Advanced Energy, Kyoto University, Uji, Kyoto, Japan.
  • Morii T; Institute of Advanced Energy, Kyoto University, Uji, Kyoto, Japan. Electronic address: t-morii@iae.kyoto-u.ac.jp.
Methods Enzymol ; 641: 183-223, 2020.
Article en En | MEDLINE | ID: mdl-32713523
Receptor-based fluorescent sensors are the representative tool for quantitative detection of target ligands. The high substrate-selectivity originated from biomacromolecule receptor is one of the advantages of this tool, but a laborious trial and error is usually required to construct sensors showing satisfactory fluorescence intensity changes without diminishing the function of parent receptor. Ribonucleopeptide (RNP) provides a scaffold of fluorescent sensors to improve such issues. RNP receptors for the ligand of interest are constructed by applying in vitro selection for RNA-derived RNP library. Simple modification of the N-terminal of peptide in RNP by an appropriate fluorophore converts the RNP receptor into the fluorescent sensor with retaining the affinity and selectivity for the substrate. In this chapter, we introduce the protocols for construction of fluorescent RNP sensors through selection from a library of fluorophore-modified RNP complex or by a structure-based modular design. Furthermore, we describe the application of covalently linked RNP sensors for simultaneous detection of multiple ligands.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Técnicas Biosensibles / Adenosina Trifosfato Idioma: En Revista: Methods Enzymol Año: 2020 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Técnicas Biosensibles / Adenosina Trifosfato Idioma: En Revista: Methods Enzymol Año: 2020 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos