Identification of polyoxometalates as inhibitors of basic fibroblast growth factor
Angiogenesis is the process of new blood vessel formation from pre-existing ones. Angiogenic factors contribute to neovascularization that takes place in angiogenesis-dependent diseases, including cancer. Inhibiting the activity of the angiogenic factors to block the angiogenesis pathways is the cur...
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| Veröffentlicht in: | Molecular bioSystems 2013-01, Vol.9 (1), p.113-120 |
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| creator | Pu, Fang Wang, Enbo Jiang, Hongyu Ren, Jinsong |
| description | Angiogenesis is the process of new blood vessel formation from pre-existing ones. Angiogenic factors contribute to neovascularization that takes place in angiogenesis-dependent diseases, including cancer. Inhibiting the activity of the angiogenic factors to block the angiogenesis pathways is the current strategy of cancer therapy. Basic fibroblast growth factor (bFGF) is regarded as one of the most important angiogenic factors. Herein, we selected polyoxometalates (POMs) with different structures to study the interactions between bFGF and POMs. The results show that POMs could bind to the protein with high affinity, causing detectable changes in conformation and biophysical properties of protein. In addition, POMs could effectively inhibit the cell proliferation induced by bFGF. Significantly, we found that the structure, size and composition of POMs play a key role in the interactions between bFGF and POMs. This study will be meaningful for future screening and design of polyoxometalate-based anticancer drugs. |
| doi_str_mv | 10.1039/c2mb25389e |
| format | Article |
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Angiogenic factors contribute to neovascularization that takes place in angiogenesis-dependent diseases, including cancer. Inhibiting the activity of the angiogenic factors to block the angiogenesis pathways is the current strategy of cancer therapy. Basic fibroblast growth factor (bFGF) is regarded as one of the most important angiogenic factors. Herein, we selected polyoxometalates (POMs) with different structures to study the interactions between bFGF and POMs. The results show that POMs could bind to the protein with high affinity, causing detectable changes in conformation and biophysical properties of protein. In addition, POMs could effectively inhibit the cell proliferation induced by bFGF. 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Angiogenic factors contribute to neovascularization that takes place in angiogenesis-dependent diseases, including cancer. Inhibiting the activity of the angiogenic factors to block the angiogenesis pathways is the current strategy of cancer therapy. Basic fibroblast growth factor (bFGF) is regarded as one of the most important angiogenic factors. Herein, we selected polyoxometalates (POMs) with different structures to study the interactions between bFGF and POMs. The results show that POMs could bind to the protein with high affinity, causing detectable changes in conformation and biophysical properties of protein. In addition, POMs could effectively inhibit the cell proliferation induced by bFGF. Significantly, we found that the structure, size and composition of POMs play a key role in the interactions between bFGF and POMs. This study will be meaningful for future screening and design of polyoxometalate-based anticancer drugs.</description><subject>Analysis of Variance</subject><subject>Binding Sites</subject><subject>Cell Proliferation - drug effects</subject><subject>Cells, Cultured</subject><subject>Circular Dichroism</subject><subject>Fibroblast Growth Factor 2 - antagonists & inhibitors</subject><subject>Fibroblast Growth Factor 2 - chemistry</subject><subject>Fibroblast Growth Factor 2 - drug effects</subject><subject>Fibroblast Growth Factor 2 - metabolism</subject><subject>Human Umbilical Vein Endothelial Cells - cytology</subject><subject>Human Umbilical Vein Endothelial Cells - drug effects</subject><subject>Human Umbilical Vein Endothelial Cells - metabolism</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein Denaturation</subject><subject>Spectrometry, Fluorescence</subject><subject>Trypsin - chemistry</subject><subject>Trypsin - metabolism</subject><subject>Tungsten Compounds - chemistry</subject><subject>Tungsten Compounds - pharmacology</subject><issn>1742-206X</issn><issn>1742-2051</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo90E9LwzAYx_EgipvTiy9AehShmj9tkxx1TB1MBFHwVp6kiYu0zUwydO_ezc2dnufw4Xf4InRO8DXBTN5o2ilaMiHNARoSXtCc4pIc7v_qfYBOYvzEmImC4GM0oIxQxmk5RC_TxvTJWachOd9n3mYL3678j-9MghaSiRnEzPVzp1zyIW6Eguh0Zp0KXrUQU_YR_HeaZxb0mpyiIwttNGe7O0Jv95PX8WM-e36Yjm9nuaaCp1woqZQmljFLFRHGgGJCV1jahuoGVwIU5qSR0grNGwZccCgrYwtDixIKy0bocru7CP5raWKqOxe1aVvojV_GmlCKuWQFlmt6taU6-BiDsfUiuA7Cqia43jSsx_Tp7q_hZI0vdrtL1ZlmT_-jsV-yoG46</recordid><startdate>20130101</startdate><enddate>20130101</enddate><creator>Pu, Fang</creator><creator>Wang, Enbo</creator><creator>Jiang, Hongyu</creator><creator>Ren, Jinsong</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20130101</creationdate><title>Identification of polyoxometalates as inhibitors of basic fibroblast growth factor</title><author>Pu, Fang ; Wang, Enbo ; Jiang, Hongyu ; Ren, Jinsong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c287t-8b9bbc1f33f2b18eeab38c609fd2cd068ab071d99f8c7d3a787a56ef4e245a4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Analysis of Variance</topic><topic>Binding Sites</topic><topic>Cell Proliferation - drug effects</topic><topic>Cells, Cultured</topic><topic>Circular Dichroism</topic><topic>Fibroblast Growth Factor 2 - antagonists & inhibitors</topic><topic>Fibroblast Growth Factor 2 - chemistry</topic><topic>Fibroblast Growth Factor 2 - drug effects</topic><topic>Fibroblast Growth Factor 2 - metabolism</topic><topic>Human Umbilical Vein Endothelial Cells - cytology</topic><topic>Human Umbilical Vein Endothelial Cells - drug effects</topic><topic>Human Umbilical Vein Endothelial Cells - metabolism</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Models, Molecular</topic><topic>Molecular Conformation</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Protein Denaturation</topic><topic>Spectrometry, Fluorescence</topic><topic>Trypsin - chemistry</topic><topic>Trypsin - metabolism</topic><topic>Tungsten Compounds - chemistry</topic><topic>Tungsten Compounds - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pu, Fang</creatorcontrib><creatorcontrib>Wang, Enbo</creatorcontrib><creatorcontrib>Jiang, Hongyu</creatorcontrib><creatorcontrib>Ren, Jinsong</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular bioSystems</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pu, Fang</au><au>Wang, Enbo</au><au>Jiang, Hongyu</au><au>Ren, Jinsong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of polyoxometalates as inhibitors of basic fibroblast growth factor</atitle><jtitle>Molecular bioSystems</jtitle><addtitle>Mol Biosyst</addtitle><date>2013-01-01</date><risdate>2013</risdate><volume>9</volume><issue>1</issue><spage>113</spage><epage>120</epage><pages>113-120</pages><issn>1742-206X</issn><eissn>1742-2051</eissn><abstract>Angiogenesis is the process of new blood vessel formation from pre-existing ones. Angiogenic factors contribute to neovascularization that takes place in angiogenesis-dependent diseases, including cancer. Inhibiting the activity of the angiogenic factors to block the angiogenesis pathways is the current strategy of cancer therapy. Basic fibroblast growth factor (bFGF) is regarded as one of the most important angiogenic factors. Herein, we selected polyoxometalates (POMs) with different structures to study the interactions between bFGF and POMs. The results show that POMs could bind to the protein with high affinity, causing detectable changes in conformation and biophysical properties of protein. In addition, POMs could effectively inhibit the cell proliferation induced by bFGF. Significantly, we found that the structure, size and composition of POMs play a key role in the interactions between bFGF and POMs. This study will be meaningful for future screening and design of polyoxometalate-based anticancer drugs.</abstract><cop>England</cop><pmid>23123725</pmid><doi>10.1039/c2mb25389e</doi><tpages>8</tpages></addata></record> |
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| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | Analysis of Variance Binding Sites Cell Proliferation - drug effects Cells, Cultured Circular Dichroism Fibroblast Growth Factor 2 - antagonists & inhibitors Fibroblast Growth Factor 2 - chemistry Fibroblast Growth Factor 2 - drug effects Fibroblast Growth Factor 2 - metabolism Human Umbilical Vein Endothelial Cells - cytology Human Umbilical Vein Endothelial Cells - drug effects Human Umbilical Vein Endothelial Cells - metabolism Humans Kinetics Models, Molecular Molecular Conformation Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Denaturation Spectrometry, Fluorescence Trypsin - chemistry Trypsin - metabolism Tungsten Compounds - chemistry Tungsten Compounds - pharmacology |
| title | Identification of polyoxometalates as inhibitors of basic fibroblast growth factor |
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