Inhibition of the Dimerization and Active Site of HIV-1 Protease by Secondary Metabolites from the Vietnamese Mushroom Ganoderma colossum

Riham Salah El Dine†‡, Ali M. El Halawany†‡, Chao-Mei Ma† and Masao Hattori*†
Institute of Natural Medicine, University of Toyama, 2630 Sugitani, Toyama 930-0194, Japan, and Department of Pharmacognosy, Faculty of Pharmacy, Cairo University, Cairo, Egypt 11562
J. Nat. Prod., 2009, 72 (11), pp 2019–2023
DOI: 10.1021/np900279u
Publication Date (Web): October 8, 2009
Copyright © 2009 The American Chemical Society and American Society of Pharmacognosy
* Corresponding author. Tel: +81-76-434-7630. Fax: +81-76-434-5060. E-mail: saibo421@inm.u-toyama.ac.jp., †

University of Toyama.

, ‡

Cairo University.

Abstract

Abstract Image

A new farnesyl hydroquinone, ganomycin I (1), was isolated along with ganomycin B (2) from the chloroform extract of the fruiting bodies of the Vietnamese mushroom Ganoderma colossum. These compounds inhibited HIV-1 protease with IC50 values of 7.5 and 1.0 μg/mL, respectively. Kinetic studies using Zhang−Poorman and Lineweaver plots revealed that compound 2 competitively inhibited the active site of the enzyme, whereas the tetracyclic triterpene schisanlactone A, previously isolated from the same fungus, was a dimerization inhibitor, with an IC50 value of 5.0 μg/mL. The previous findings were also confirmed by the virtual docking of both compounds with HIV-1 protease crystal structure.

View: Full Text HTML | Hi-Res PDF | PDF w/ Links

Tools

SciFinder Links

SciFinder subscribers: Click to sign in | Not a SciFinder subscriber? Learn more at www.cas.org

Explore by:

History

  • Published In Issue November 30, 2009
  • Article ASAPOctober 08, 2009
  • Received: May 10, 2009

Recommend & Share

Related Content

Other ACS content by these authors: