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

Authors: Yeh S.F.¹; Pan W.¹; Ong G.T.²; Chiou A.J.³; Chuang C.C.²; Chiou S.H.^{2, 3}; Wu S.H.^{2, 3}

Source: Biochemical and Biophysical Research Communications, Volume 229, Number 1, December 1996 , pp. 65-72(8)

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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.

Language: English

Document Type: Research article

Affiliations: 1: Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan 2: Institute of Biological Chemistry, Academia Sinica 3: Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan

Publication date: 1996-12-01