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Synthesis of two fluorescent GTPS molecules and their biological relevance

  1. Author:
    Trans, Denise J.
    Bai, Ruoli
    Addison, J. Bennet
    Liu, Ruiwu
    Hamel, Ernest
    Coleman, Matthew A.
    Henderson, Paul T.

  2. Author Address

    Univ Calif Davis, Dept Internal Med, Davis, CA 95616 USA.Univ Calif Davis, UC Davis Comprehens Canc Ctr, Davis, CA 95616 USA.NCI, Screening Technol Branch, Dev Therapeut Program, Div Canc Treatment & Diag,Frederick Natl Lab Canc, Frederick, MD 21701 USA.Univ Calif Davis, Nucl Magnet Resonance Facil, Davis, CA 95616 USA.Univ Calif Davis, Dept Biochem & Mol Med, Davis, CA 95616 USA.Univ Calif Davis, Dept Radiat Oncol, Davis, CA 95616 USA.Lawrence Livermore Natl Lab, Livermore, CA USA.
    1. Year: 2017
  2. Journal: NUCLEOSIDES NUCLEOTIDES & NUCLEIC ACIDS
  3. TAYLOR & FRANCIS INC,
    1. 36
    2. 6
    3. Pages: 379-391
  5. Type of Article: Article
  6. ISSN: 1525-7770
  1. Abstract:

    Fluorescent GTP analogues are utilized for an assortment of nucleic acid and protein characterization studies. Non-hydrolysable analogues such as GTPS offer the advantage of keeping proteins in a GTP-bound conformation due to their resistance to hydrolysis into GDP. Two novel fluorescent GTPS molecules were developed by linking fluorescein and tetramethylrhodamine to the -thiophosphate of GTPS. Chemical and biological analysis of these two compounds revealed their successful synthesis and ability to bind to the nucleotide-binding site of tubulin. These two new fluorescent non-hydrolysable nucleotides offer new possibilities for biophysical and biochemical characterization of GTP-binding proteins.

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External Sources

  1. View Full Text
  2. DOI: 10.1080/15257770.2016.1231320
  3. View record in Web of Science®
  4. WOS: 000402655600001

Library Notes

  1. Fiscal Year: FY2016-2017
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