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N1-Propargylguanosine Modified mRNA Cap Analogs: Synthesis, Reactivity, and Applications to the Study of Cap-Binding Proteins.
Kopcial, Michal; Wojtczak, Blazej A; Kasprzyk, Renata; Kowalska, Joanna; Jemielity, Jacek.
Afiliación
  • Kopcial M; College of Inter-Faculty Individual Studies in Mathematics and Natural Sciences, University of Warsaw, S. Banacha 2c, 02-097 Warsaw, Poland. m.kopcial@cent.uw.edu.pl.
  • Wojtczak BA; Centre of New Technologies, University of Warsaw; S. Banacha 2c, 02-097 Warsaw, Poland. m.kopcial@cent.uw.edu.pl.
  • Kasprzyk R; Faculty of Physics, University of Warsaw; L. Pasteura 5, 02-093 Warsaw, Poland. m.kopcial@cent.uw.edu.pl.
  • Kowalska J; Centre of New Technologies, University of Warsaw; S. Banacha 2c, 02-097 Warsaw, Poland. blazej.wojtczak@cent.uw.edu.pl.
  • Jemielity J; College of Inter-Faculty Individual Studies in Mathematics and Natural Sciences, University of Warsaw, S. Banacha 2c, 02-097 Warsaw, Poland. rkasprzyk@biogeo.uw.edu.pl.
Molecules ; 24(10)2019 May 17.
Article en En | MEDLINE | ID: mdl-31108861
The mRNA 5' cap consists of N7-methylguanosine bound by a 5',5'-triphosphate bridge to the first nucleotide of the transcript. The cap interacts with various specific proteins and participates in all key mRNA-related processes, which may be of therapeutic relevance. There is a growing demand for new biophysical and biochemical methods to study cap-protein interactions and identify the factors which inhibit them. The development of such methods can be aided by the use of properly designed fluorescent molecular probes. Herein, we synthesized a new class of m7Gp3G cap derivatives modified with an alkyne handle at the N1-position of guanosine and, using alkyne-azide cycloaddition, we functionalized them with fluorescent tags to obtain potential probes. The cap derivatives and probes were evaluated in the context of two cap-binding proteins, eukaryotic translation initiation factor (eIF4E) and decapping scavenger (DcpS). Biochemical and biophysical studies revealed that N1-propargyl moiety did not significantly disturb cap-protein interaction. The fluorescent properties of the probes turned out to be in line with microscale thermophoresis (MST)-based binding assays.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Análogos de Caperuza de ARN / Proteínas de Unión a Caperuzas de ARN Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2019 Tipo del documento: Article País de afiliación: Polonia

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Análogos de Caperuza de ARN / Proteínas de Unión a Caperuzas de ARN Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2019 Tipo del documento: Article País de afiliación: Polonia