Binding of Antitumor Compounds to Wheat Protein
Binding of porphyrins to biological macromolecules is important to be studied as an approach to keeping them in stable, effective and safe dosage forms. In this work we show the interaction of three porphyrin compounds: Hematoporphyrin IX, Mn- and Fe- porphyrins with plant lectin Wheat germ agglutin...
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| Veröffentlicht in: | Biotechnology, biotechnological equipment biotechnological equipment, 2013, Vol.27 (3), p.3857-3860 |
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| container_title | Biotechnology, biotechnological equipment |
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| creator | Petrova, Lidiya Kulina, Hristina Trifonov, Anton Russev, George Marinova, Kristiana Bogoeva, Vanya |
| description | Binding of porphyrins to biological macromolecules is important to be studied as an approach to keeping them in stable, effective and safe dosage forms. In this work we show the interaction of three porphyrin compounds: Hematoporphyrin IX, Mn- and Fe- porphyrins with plant lectin Wheat germ agglutinin (WGA). Porphyrin binding to WGA was monitored by the changes in the intrinsic protein fluorescence. Conformational changes due to the formation of WGA-porphyrin complexes, were shown by the hyperbolic binding curves. The calculated dissociation constants K
D
(0.16 μM to 0.24 μM) indicate high affinity of WGA for the three porphyrins. Most probably they occupy the same high affinity sites. In conclusion, since WGA binds cancer cells and interacts with antitumor compounds, it could be useful as a drug delivery molecule. |
| doi_str_mv | 10.5504/BBEQ.2013.0025 |
| format | Article |
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D
(0.16 μM to 0.24 μM) indicate high affinity of WGA for the three porphyrins. Most probably they occupy the same high affinity sites. In conclusion, since WGA binds cancer cells and interacts with antitumor compounds, it could be useful as a drug delivery molecule.</description><identifier>ISSN: 1310-2818</identifier><identifier>EISSN: 1314-3530</identifier><identifier>DOI: 10.5504/BBEQ.2013.0025</identifier><language>eng</language><publisher>Sofia: Taylor & Francis</publisher><subject>Affinity ; Antitumor agents ; Binding ; Drug delivery ; Drug delivery systems ; Fluorescence ; Macromolecules ; Manganese ; Porphyrins ; protein ; Proteins ; Triticum aestivum ; Wheat ; Wheat germ ; Wheat germ agglutinin</subject><ispartof>Biotechnology, biotechnological equipment, 2013, Vol.27 (3), p.3857-3860</ispartof><rights>2013 Taylor and Francis Group, LLC 2013</rights><rights>2013 Taylor and Francis Group, LLC</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c350t-694826386cdf4c7d922059b95238b9bf478176b2433b450b17b3068286e39b3d3</citedby><cites>FETCH-LOGICAL-c350t-694826386cdf4c7d922059b95238b9bf478176b2433b450b17b3068286e39b3d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids></links><search><creatorcontrib>Petrova, Lidiya</creatorcontrib><creatorcontrib>Kulina, Hristina</creatorcontrib><creatorcontrib>Trifonov, Anton</creatorcontrib><creatorcontrib>Russev, George</creatorcontrib><creatorcontrib>Marinova, Kristiana</creatorcontrib><creatorcontrib>Bogoeva, Vanya</creatorcontrib><title>Binding of Antitumor Compounds to Wheat Protein</title><title>Biotechnology, biotechnological equipment</title><description>Binding of porphyrins to biological macromolecules is important to be studied as an approach to keeping them in stable, effective and safe dosage forms. In this work we show the interaction of three porphyrin compounds: Hematoporphyrin IX, Mn- and Fe- porphyrins with plant lectin Wheat germ agglutinin (WGA). Porphyrin binding to WGA was monitored by the changes in the intrinsic protein fluorescence. Conformational changes due to the formation of WGA-porphyrin complexes, were shown by the hyperbolic binding curves. The calculated dissociation constants K
D
(0.16 μM to 0.24 μM) indicate high affinity of WGA for the three porphyrins. Most probably they occupy the same high affinity sites. In conclusion, since WGA binds cancer cells and interacts with antitumor compounds, it could be useful as a drug delivery molecule.</description><subject>Affinity</subject><subject>Antitumor agents</subject><subject>Binding</subject><subject>Drug delivery</subject><subject>Drug delivery systems</subject><subject>Fluorescence</subject><subject>Macromolecules</subject><subject>Manganese</subject><subject>Porphyrins</subject><subject>protein</subject><subject>Proteins</subject><subject>Triticum aestivum</subject><subject>Wheat</subject><subject>Wheat germ</subject><subject>Wheat germ agglutinin</subject><issn>1310-2818</issn><issn>1314-3530</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp1kM9LwzAUgIMoOKdXzwUvXtq9_GrT4zbmDxiooHgMTZtqRpvMJEX237tungRP7x2-7_H4ELrGkHEObLZYrF4yAphmAISfoAmmmKWUUzg97JASgcU5ughhA1AA4GKCZgtjG2M_EtcmcxtNHHrnk6Xrt26wTUiiS94_dRWTZ--iNvYSnbVVF_TV75yit7vV6_IhXT_dPy7n67SmHGKal0yQnIq8blpWF01JCPBSlZxQoUrVskLgIleEUaoYB4ULRSEXROSaloo2dIpuj3e33n0NOkTZm1DrrqusdkOQmDMghGEge_TmD7pxg7f77yQhpMw55gcqO1K1dyF43cqtN33ldxKDHPvJsZ8c-8mx314oj4KxrfN99e1818hY7TrnW1_Z2gRJ_3F_ADB-cb8</recordid><startdate>2013</startdate><enddate>2013</enddate><creator>Petrova, Lidiya</creator><creator>Kulina, Hristina</creator><creator>Trifonov, Anton</creator><creator>Russev, George</creator><creator>Marinova, Kristiana</creator><creator>Bogoeva, Vanya</creator><general>Taylor & Francis</general><general>Taylor & Francis Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QO</scope><scope>7ST</scope><scope>7XB</scope><scope>8FD</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>M2O</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>SOI</scope></search><sort><creationdate>2013</creationdate><title>Binding of Antitumor Compounds to Wheat Protein</title><author>Petrova, Lidiya ; 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In this work we show the interaction of three porphyrin compounds: Hematoporphyrin IX, Mn- and Fe- porphyrins with plant lectin Wheat germ agglutinin (WGA). Porphyrin binding to WGA was monitored by the changes in the intrinsic protein fluorescence. Conformational changes due to the formation of WGA-porphyrin complexes, were shown by the hyperbolic binding curves. The calculated dissociation constants K
D
(0.16 μM to 0.24 μM) indicate high affinity of WGA for the three porphyrins. Most probably they occupy the same high affinity sites. In conclusion, since WGA binds cancer cells and interacts with antitumor compounds, it could be useful as a drug delivery molecule.</abstract><cop>Sofia</cop><pub>Taylor & Francis</pub><doi>10.5504/BBEQ.2013.0025</doi><tpages>4</tpages></addata></record> |
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| subjects | Affinity Antitumor agents Binding Drug delivery Drug delivery systems Fluorescence Macromolecules Manganese Porphyrins protein Proteins Triticum aestivum Wheat Wheat germ Wheat germ agglutinin |
| title | Binding of Antitumor Compounds to Wheat Protein |
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