Effects of triterpenoids and flavonoids isolated from Alnus firma on HIV-1 viral enzymes

Arch Pharm Res. 2007 Jul;30(7):820-6. doi: 10.1007/BF02978831.

Abstract

Triterpenoids and flavonoids isolated from Alnus firma S. Z. were found to inhibit HIV-1 virus replication and controlled its essential enzymes. In this study, the inhibition of HIV-1 viral replication and its essential enzymes, such as reverse transcriptase, protease and alpha-glucosidase, were observed using 18 Korean plant extracts. Among the extracts, the methanol extract of Alnus firma leaves showed potent inhibition against the HIV-1 induced cytopathic effect (CPE) in MT-4 cells on microscopic observation (the minimum concentration for complete inhibition of HIV-1 induced CPE, IC=50 microg/mL). Thus, 14 compounds were isolated and identified from the methanol extract of Alnus firma leaves. Of these compounds, the alnustic acid methyl ester exhibited inhibition against HIV-1 protease, with an IC50 of 15.8 microM, and quercetin, quercitrin and myricetin 3-O-beta-D-galactopyranoside displayed inhibition against HIV-1 reverse transcriptase, all with IC50 values of 60 microM. Based on these results, the viral replication inhibition of the methanol extract of Alnus firma leaves was adjudged to be acutely related to the protease inhibition activation of the alnustic acid methyl ester as well as the reverse transcriptase inhibition activation of flavonoids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alnus / chemistry*
  • Anti-HIV Agents / isolation & purification*
  • Anti-HIV Agents / pharmacology
  • Cell Line
  • Cell Survival
  • Chromatography, High Pressure Liquid
  • Cytopathogenic Effect, Viral
  • Flavonoids / isolation & purification*
  • Flavonoids / pharmacology
  • Glycoside Hydrolase Inhibitors
  • HIV Protease / metabolism
  • HIV Protease Inhibitors / isolation & purification
  • HIV Protease Inhibitors / pharmacology
  • HIV Reverse Transcriptase / antagonists & inhibitors
  • HIV-1* / drug effects
  • HIV-1* / enzymology
  • HIV-1* / physiology
  • Humans
  • Molecular Structure
  • Nuclear Magnetic Resonance, Biomolecular
  • Triterpenes / isolation & purification*
  • Triterpenes / pharmacology
  • Virus Replication / drug effects
  • alpha-Glucosidases

Substances

  • Anti-HIV Agents
  • Flavonoids
  • Glycoside Hydrolase Inhibitors
  • HIV Protease Inhibitors
  • Triterpenes
  • HIV Reverse Transcriptase
  • glucosidase I
  • alpha-Glucosidases
  • HIV Protease