A sorghum xylanase inhibitor-like protein with highly potent antifungal, antitumor and HIV-1 reverse transcriptase inhibitory activities.
Identifieur interne : 001166 ( PubMed/Corpus ); précédent : 001165; suivant : 001167A sorghum xylanase inhibitor-like protein with highly potent antifungal, antitumor and HIV-1 reverse transcriptase inhibitory activities.
Auteurs : Peng Lin ; Jack Ho Wong ; Tzi Bun Ng ; Vincent Sai Man Ho ; Lixin XiaSource :
- Food chemistry [ 1873-7072 ] ; 2013.
English descriptors
- KwdEn :
- Animals, Antifungal Agents (chemistry), Antifungal Agents (isolation & purification), Antifungal Agents (pharmacology), Antineoplastic Agents, Phytogenic (chemistry), Antineoplastic Agents, Phytogenic (isolation & purification), Antineoplastic Agents, Phytogenic (pharmacology), Cell Line, Tumor, Cell Proliferation (drug effects), Endo-1,4-beta Xylanases (antagonists & inhibitors), Endo-1,4-beta Xylanases (chemistry), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (isolation & purification), Enzyme Inhibitors (pharmacology), Fungi (drug effects), HIV Reverse Transcriptase (antagonists & inhibitors), HIV Reverse Transcriptase (chemistry), Humans, Kinetics, Mice, Plant Proteins (chemistry), Plant Proteins (isolation & purification), Plant Proteins (pharmacology), Protein Stability, Seeds (chemistry), Sorghum (chemistry).
- MESH :
- chemical , antagonists & inhibitors : Endo-1,4-beta Xylanases, HIV Reverse Transcriptase.
- chemical , chemistry : Antifungal Agents, Antineoplastic Agents, Phytogenic, Endo-1,4-beta Xylanases, Enzyme Inhibitors, HIV Reverse Transcriptase, Plant Proteins.
- chemical , isolation & purification : Antifungal Agents, Antineoplastic Agents, Phytogenic, Enzyme Inhibitors, Plant Proteins.
- chemical , pharmacology : Antifungal Agents, Antineoplastic Agents, Phytogenic, Enzyme Inhibitors, Plant Proteins.
- chemistry : Seeds, Sorghum.
- drug effects : Cell Proliferation, Fungi.
- Animals, Cell Line, Tumor, Humans, Kinetics, Mice, Protein Stability.
Abstract
A 25-kDa protein, with an N-terminal amino acid sequence homologous to that of xylanase inhibitor and designated as xylanase inbibitor-like protein (XILP) was purified from sorghum seeds. The isolation protocol consisted of affinity chromatography, ion exchange chromatography, and gel filtration. XILP inhibited mycelial growth in various phytopathogenic fungi. The antifungal activity was thermostable and pH-stable. XILP inhibited proliferation of various cancer cell lines but did not do so in human embryonic liver (WRL 68) cells. There was no mitogenic activity toward mouse splenocytes. XILP reduced the activity of HIV-1 reverse transcriptase with an IC50 of 11.1μM, but lacked inhibitory activity toward HIV-1 integrase and SARS coronavirus proteinase. In conclusion, sorghum XILP is thermostable and pH stable and exhibits potent antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities.
DOI: 10.1016/j.foodchem.2013.04.013
PubMed: 23871041
Links to Exploration step
pubmed:23871041Le document en format XML
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<term>Humans</term>
<term>Kinetics</term>
<term>Mice</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (isolation & purification)</term>
<term>Plant Proteins (pharmacology)</term>
<term>Protein Stability</term>
<term>Seeds (chemistry)</term>
<term>Sorghum (chemistry)</term>
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<front><div type="abstract" xml:lang="en">A 25-kDa protein, with an N-terminal amino acid sequence homologous to that of xylanase inhibitor and designated as xylanase inbibitor-like protein (XILP) was purified from sorghum seeds. The isolation protocol consisted of affinity chromatography, ion exchange chromatography, and gel filtration. XILP inhibited mycelial growth in various phytopathogenic fungi. The antifungal activity was thermostable and pH-stable. XILP inhibited proliferation of various cancer cell lines but did not do so in human embryonic liver (WRL 68) cells. There was no mitogenic activity toward mouse splenocytes. XILP reduced the activity of HIV-1 reverse transcriptase with an IC50 of 11.1μM, but lacked inhibitory activity toward HIV-1 integrase and SARS coronavirus proteinase. In conclusion, sorghum XILP is thermostable and pH stable and exhibits potent antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities. </div>
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<Abstract><AbstractText>A 25-kDa protein, with an N-terminal amino acid sequence homologous to that of xylanase inhibitor and designated as xylanase inbibitor-like protein (XILP) was purified from sorghum seeds. The isolation protocol consisted of affinity chromatography, ion exchange chromatography, and gel filtration. XILP inhibited mycelial growth in various phytopathogenic fungi. The antifungal activity was thermostable and pH-stable. XILP inhibited proliferation of various cancer cell lines but did not do so in human embryonic liver (WRL 68) cells. There was no mitogenic activity toward mouse splenocytes. XILP reduced the activity of HIV-1 reverse transcriptase with an IC50 of 11.1μM, but lacked inhibitory activity toward HIV-1 integrase and SARS coronavirus proteinase. In conclusion, sorghum XILP is thermostable and pH stable and exhibits potent antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities. </AbstractText>
<CopyrightInformation>Copyright © 2013 Elsevier Ltd. All rights reserved.</CopyrightInformation>
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