Mass Spectrometric Characterization of HIV-1 Reverse Transcriptase Interactions with Non-nucleoside Reverse Transcriptase Inhibitors

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Author(s)

    • Uchiyama Susumu
    • Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences|Department of Biotechnology, Graduate School of Engineering, Osaka University
    • Hannongbua Supa
    • Department of Chemistry, Faculty of Science, Kasetsart University|Center of Nanotechnology, Kasetsart University
    • Kato Koichi
    • Institute for Molecular Science, National Institutes of Natural Sciences|Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences

Abstract

Non-nucleoside reverse transcriptase inhibitors (NNRTIs) of human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) have been developed for the treatment of acquired immunodeficiency syndrome. HIV-1 RT binding to NNRTIs has been characterized by various biophysical techniques. However, these techniques are often hampered by the low water solubility of the inhibitors, such as the current promising diarylpyrimidine-based inhibitors rilpivirine and etravirine. Hence, a conventional and rapid method that requires small sample amounts is desirable for studying NNRTIs with low water solubility. Here we successfully applied a recently developed mass spectrometric technique under non-denaturing conditions to characterize the interactions between the heterodimeric HIV-1 RT enzyme and NNRTIs with different inhibitory activities. Our data demonstrate that mass spectrometry serves as a semi-quantitative indicator of NNRTI binding affinity for HIV-1 RT using low and small amounts of samples, offering a new high-throughput screening tool for identifying novel RT inhibitors as anti-HIV drugs.

Journal

  • Biological and Pharmaceutical Bulletin

    Biological and Pharmaceutical Bulletin 39(3), 450-454, 2016

    The Pharmaceutical Society of Japan

Codes

  • NII Article ID (NAID)
    130005132309
  • NII NACSIS-CAT ID (NCID)
    AA10885497
  • Text Lang
    ENG
  • ISSN
    0918-6158
  • NDL Article ID
    027133934
  • NDL Call No.
    Z53-V41
  • Data Source
    NDL  J-STAGE 
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