tetano
Editor, Senior Moderator
FEBS J. 2013 Aug 26. doi: 10.1111/febs.12503. [Epub ahead of print]
Structure-activity relationship analysis of curcumin analogues on anti-influenza virus activity.
Ou JL, Mizushina Y, Wang SY, Chuang DY, Nadar M, Hsu WL.
Source
Graduate Institute of Microbiology and Public Health, National Chung Hsing University, 250 Kuo Kuang Road, Taichung, 402, Taiwan.
Abstract
Curcumin is a commonly used colouring agent and spice in food. Previously, we reported curcumin inhibits type A influenza virus (IAV) infection by interfering with the viral HA activity. To search for a stable curcumin analogue with potent anti-IAV activity and to investigate the structure contributing to its anti-IAV activity, a comparative analysis of structural and functional analogues of curcumin (Cur), such as tetrahydrocurcumin (THC), and petasiphenol (Pet), was performed in the current study. The result of time-of-drug addition tests indicated that these curcuminoids were able to inhibit IAV production in cell cultures. Noticeably, Pet and THC inhibit IAV to a less extent than curcumin that in line with their effect on reducing plaque formation when IAV was treated with curcumin analogues prior to infection. Surprisingly, both THC and Pet did not harbour HA inhibitory effect. It should be noted that the structure of Pet and THC differs from curcumin in the number of double bonds present in the central seven-carbon chain, and structure modelling of curcumin analogues indicates that the conformations of THC and Pet are distinct from that of curcumin. Moreover, simulation docking of curcumin with HA structure revealed that curcumin binds to the region constituting Sialic acid anchoring residues that supports the results on HI assay. Collectively, structure-activity relationship analyses indicate that presence of the double bonds in the central seven-carbon chain enhanced the curcumin-dependent anti-IAV activity and curcumin might interfere with IAV entry by its interaction with the receptor binding region of viral HA protein. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
KEYWORDS:
Curcumin, influenza virus, petasiphenol, simulation docking, structure analogue, structure-activity relationship, tetrahydrocurcumin
PMID:
24034558
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24034558
Structure-activity relationship analysis of curcumin analogues on anti-influenza virus activity.
Ou JL, Mizushina Y, Wang SY, Chuang DY, Nadar M, Hsu WL.
Source
Graduate Institute of Microbiology and Public Health, National Chung Hsing University, 250 Kuo Kuang Road, Taichung, 402, Taiwan.
Abstract
Curcumin is a commonly used colouring agent and spice in food. Previously, we reported curcumin inhibits type A influenza virus (IAV) infection by interfering with the viral HA activity. To search for a stable curcumin analogue with potent anti-IAV activity and to investigate the structure contributing to its anti-IAV activity, a comparative analysis of structural and functional analogues of curcumin (Cur), such as tetrahydrocurcumin (THC), and petasiphenol (Pet), was performed in the current study. The result of time-of-drug addition tests indicated that these curcuminoids were able to inhibit IAV production in cell cultures. Noticeably, Pet and THC inhibit IAV to a less extent than curcumin that in line with their effect on reducing plaque formation when IAV was treated with curcumin analogues prior to infection. Surprisingly, both THC and Pet did not harbour HA inhibitory effect. It should be noted that the structure of Pet and THC differs from curcumin in the number of double bonds present in the central seven-carbon chain, and structure modelling of curcumin analogues indicates that the conformations of THC and Pet are distinct from that of curcumin. Moreover, simulation docking of curcumin with HA structure revealed that curcumin binds to the region constituting Sialic acid anchoring residues that supports the results on HI assay. Collectively, structure-activity relationship analyses indicate that presence of the double bonds in the central seven-carbon chain enhanced the curcumin-dependent anti-IAV activity and curcumin might interfere with IAV entry by its interaction with the receptor binding region of viral HA protein. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
KEYWORDS:
Curcumin, influenza virus, petasiphenol, simulation docking, structure analogue, structure-activity relationship, tetrahydrocurcumin
PMID:
24034558
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24034558