Study of structure-activity correlation in destruxins, a class of cyclodepsipeptides possessing suppressive effect on the generation of hepatitis B virus surface antigen in human hepatoma cells.

Abstract	A new destruxin [destruxin E2 chlorohydrin] was isolated from the culture medium of Metarrhizium anisopliae and its structure was determined by NMR spectroscopy and mass spectrometry. As compared with other destruxins, the new destruxin showed a lower suppressive activity on the production of hepatitis B virus surface antigen in human hepatoma Hep3B cells. NMR study coupled with molecular modeling by computer graphics has revealed that the hydrophobicity nature of the convex surface characteristic of all destruxin molecules plays an important role in their biological activity.
Authors	S F Yeh, W Pan, G T Ong, A J Chiou, C C Chuang, S H Chiou, S H Wu
Journal	Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 229 Issue 1 Pg. 65-72 (Dec 04 1996) ISSN: 0006-291X [Print] United States
PMID	8954084 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Antiviral Agents Depsipeptides Hepatitis B Surface Antigens Peptides, Cyclic destruxin E2 chlorohydrin
Topics	Antiviral Agents (chemistry, pharmacology) Carcinoma, Hepatocellular (virology) Computer Simulation Crystallography, X-Ray Depsipeptides Hepatitis B Surface Antigens (biosynthesis) Hepatitis B virus (drug effects) Humans Magnetic Resonance Spectroscopy Mitosporic Fungi (chemistry) Models, Molecular Peptides, Cyclic (chemistry, pharmacology) Protein Conformation Structure-Activity Relationship

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