Sialidase inhibitory activity of diarylnonanoid and neolignan compounds extracted from the seeds of Myristica fragrans

Bioorg Med Chem Lett. 2017 Jul 15;27(14):3060-3064. doi: 10.1016/j.bmcl.2017.05.055. Epub 2017 May 18.

Abstract

Sialidases are key virulence factors that remove sialic acid from host cell surface glycans, thus unmasking receptors to facilitate bacterial adherence and colonization. In this study, we report the isolation and characterization of novel inhibitors of the Streptococcus pneumoniae sialidases NanA, NanB, and NanC from Myristica fragrans seeds. Of the isolated compounds (1-12), malabaricone C showed the most pneumococcal sialidases inhibition (IC50 of 0.3μM for NanA, 3.6μM for NanB, and 2.9μM for NanC). These results suggested that malabaricone C and neolignans could be potential agents for combating S. pneumoniae infection agents.

Keywords: Malabaricone C; Myristica fragrans; NanA; NanB; Sialidase.

MeSH terms

  • Enzyme Activation / drug effects
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / isolation & purification
  • Enzyme Inhibitors / pharmacology*
  • Inhibitory Concentration 50
  • Kinetics
  • Lignans / chemistry
  • Lignans / isolation & purification
  • Lignans / pharmacology*
  • Myristica / chemistry*
  • Myristica / metabolism
  • Neuraminidase / antagonists & inhibitors*
  • Neuraminidase / metabolism
  • Plant Extracts / chemistry
  • Plant Extracts / isolation & purification
  • Plant Extracts / pharmacology*
  • Protein Isoforms / antagonists & inhibitors
  • Protein Isoforms / metabolism
  • Resorcinols / chemical synthesis
  • Resorcinols / isolation & purification
  • Resorcinols / pharmacology
  • Seeds / chemistry
  • Seeds / metabolism
  • Streptococcus pneumoniae / drug effects
  • Streptococcus pneumoniae / enzymology

Substances

  • Enzyme Inhibitors
  • Lignans
  • Plant Extracts
  • Protein Isoforms
  • Resorcinols
  • malabaricone C
  • Neuraminidase