The affinity of RSK for cylitol analogues of SL0101 is critically dependent on the B-ring C-4'-hydroxy

  • Chem Commun (Camb). 2020 Mar 10;56(20):3058-3060. doi: 10.1039/d0cc00128g.
Yu Li  1 ,  Pedro Seber  2 ,  Eric B Wright  3 ,  Sharia Yasmin  4 ,  Deborah A Lannigan  5 ,  George A O'Doherty  1
Affiliations
  • 1. Department of Chemistry and Chemical Biology, Northeastern University, Boston, MA 02115, USA. [email protected].
  • 2. Departments of Pathology, Microbiology & Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. [email protected].
  • 3. Biomedical Engineering, Nashville, TN 37232, USA.
  • 4. Cell & Developmental Biology, Nashville, TN 37232, USA.
  • 5. Departments of Pathology, Microbiology & Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. [email protected] and Biomedical Engineering, Nashville, TN 37232, USA and Cell & Developmental Biology, Nashville, TN 37232, USA.
PMID: 32048692 DOI: 10.1039/d0cc00128g
Abstract

Five cyclitol analogues of SL0101 with variable substitution at the C-4' position (i.e., OH, Cl, F, H, OMe) were synthesized. The series of analogues were evaluated for their ability to inhibit p90 ribosomal S6 kinase (RSK) activity. The study demonstrated the importance of the B-ring C-4' hydroxy group for RSK1/2 inhibition.

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