Construction of anti-EGFR immunoliposomes via folate–folate binding protein affinity
A novel method for synthesis of anti-EGFR immunoliposomes using folate–folate binding protein (FBP) affinity is described. An anti-EGFR antibody (cetuximab or C225) was covalently linked to FBP via a thioether bond. Liposomes incorporating a lipophilic folate derivative (folate-PEG-cholesterol) were...
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| Veröffentlicht in: | International journal of pharmaceutics 2007-05, Vol.336 (2), p.276-283 |
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| creator | Pan, Xiaogang Lee, Robert J. |
| description | A novel method for synthesis of anti-EGFR immunoliposomes using folate–folate binding protein (FBP) affinity is described. An anti-EGFR antibody (cetuximab or C225) was covalently linked to FBP via a thioether bond. Liposomes incorporating a lipophilic folate derivative (folate-PEG-cholesterol) were prepared by polycarbonate membrane extrusion. Anti-EGFR immunoliposomes were then obtained by combining FBP-C225 and folate-liposomes and evaluated for uptake and cytotoxicity in EGFR-overexpressing U87 human glioblastoma cells. Anti-EGFR immunoliposomes constructed via folate–FBP affinity exhibited excellent stability under physiological pH, and quickly released the bound FBP-C225 upon low pH (pH 3.5) treatment. Flow cytometry and fluorescence microscopy showed similar receptor-specific binding and internalization for both folate–FBP affinity-coupled and covalently coupled C225-immunoliposomes, but not for the non-targeted IgG-immunoliposomes. C225-immunoliposomes loaded with anticancer drug doxorubicin were more cytotoxic than non-targeted immunoliposomes in EGFR-overexpressing U87 glioma cells. Folate–FBP affinity is a potential method for construction of immunoliposomes and may have applications in synthesis of targeted drug carriers in general. |
| doi_str_mv | 10.1016/j.ijpharm.2006.12.007 |
| format | Article |
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An anti-EGFR antibody (cetuximab or C225) was covalently linked to FBP via a thioether bond. Liposomes incorporating a lipophilic folate derivative (folate-PEG-cholesterol) were prepared by polycarbonate membrane extrusion. Anti-EGFR immunoliposomes were then obtained by combining FBP-C225 and folate-liposomes and evaluated for uptake and cytotoxicity in EGFR-overexpressing U87 human glioblastoma cells. Anti-EGFR immunoliposomes constructed via folate–FBP affinity exhibited excellent stability under physiological pH, and quickly released the bound FBP-C225 upon low pH (pH 3.5) treatment. Flow cytometry and fluorescence microscopy showed similar receptor-specific binding and internalization for both folate–FBP affinity-coupled and covalently coupled C225-immunoliposomes, but not for the non-targeted IgG-immunoliposomes. C225-immunoliposomes loaded with anticancer drug doxorubicin were more cytotoxic than non-targeted immunoliposomes in EGFR-overexpressing U87 glioma cells. Folate–FBP affinity is a potential method for construction of immunoliposomes and may have applications in synthesis of targeted drug carriers in general.</description><identifier>ISSN: 0378-5173</identifier><identifier>EISSN: 1873-3476</identifier><identifier>DOI: 10.1016/j.ijpharm.2006.12.007</identifier><identifier>PMID: 17212981</identifier><identifier>CODEN: IJPHDE</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject><![CDATA[Antibodies, Monoclonal - administration & dosage ; Antibodies, Monoclonal - pharmacology ; Antibodies, Monoclonal, Humanized ; Antineoplastic Agents - administration & dosage ; Antineoplastic Agents - pharmacology ; Biological and medical sciences ; Biological Transport ; Carrier Proteins - administration & dosage ; Carrier Proteins - pharmacology ; Cell Line, Tumor ; Cetuximab ; Doxorubicin - administration & dosage ; Doxorubicin - pharmacology ; Drug Delivery Systems ; Drug Stability ; Drug targeting ; EGF receptor ; Flow Cytometry ; Folate ; Folate binding protein ; Folate Receptors, GPI-Anchored ; Folic Acid ; General pharmacology ; Glioblastoma ; Humans ; Hydrogen-Ion Concentration ; Immunoconjugates - administration & dosage ; Immunoconjugates - pharmacology ; Immunoliposomes ; Liposomes ; Medical sciences ; Microscopy, Fluorescence ; Pharmaceutical technology. 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Drug treatments ; Polycarboxylate Cement ; Receptor, Epidermal Growth Factor - drug effects ; Receptor, Epidermal Growth Factor - immunology ; Receptor, Epidermal Growth Factor - metabolism ; Receptors, Cell Surface - administration & dosage]]></subject><ispartof>International journal of pharmaceutics, 2007-05, Vol.336 (2), p.276-283</ispartof><rights>2006 Elsevier B.V.</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-e85f03c87d598604f39013408f4d0c0f55ad8d147ef72a5c376eb5ef1e8005e93</citedby><cites>FETCH-LOGICAL-c393t-e85f03c87d598604f39013408f4d0c0f55ad8d147ef72a5c376eb5ef1e8005e93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijpharm.2006.12.007$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18752970$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17212981$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pan, Xiaogang</creatorcontrib><creatorcontrib>Lee, Robert J.</creatorcontrib><title>Construction of anti-EGFR immunoliposomes via folate–folate binding protein affinity</title><title>International journal of pharmaceutics</title><addtitle>Int J Pharm</addtitle><description>A novel method for synthesis of anti-EGFR immunoliposomes using folate–folate binding protein (FBP) affinity is described. An anti-EGFR antibody (cetuximab or C225) was covalently linked to FBP via a thioether bond. Liposomes incorporating a lipophilic folate derivative (folate-PEG-cholesterol) were prepared by polycarbonate membrane extrusion. Anti-EGFR immunoliposomes were then obtained by combining FBP-C225 and folate-liposomes and evaluated for uptake and cytotoxicity in EGFR-overexpressing U87 human glioblastoma cells. Anti-EGFR immunoliposomes constructed via folate–FBP affinity exhibited excellent stability under physiological pH, and quickly released the bound FBP-C225 upon low pH (pH 3.5) treatment. Flow cytometry and fluorescence microscopy showed similar receptor-specific binding and internalization for both folate–FBP affinity-coupled and covalently coupled C225-immunoliposomes, but not for the non-targeted IgG-immunoliposomes. C225-immunoliposomes loaded with anticancer drug doxorubicin were more cytotoxic than non-targeted immunoliposomes in EGFR-overexpressing U87 glioma cells. Folate–FBP affinity is a potential method for construction of immunoliposomes and may have applications in synthesis of targeted drug carriers in general.</description><subject>Antibodies, Monoclonal - administration & dosage</subject><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Antibodies, Monoclonal, Humanized</subject><subject>Antineoplastic Agents - administration & dosage</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Biological Transport</subject><subject>Carrier Proteins - administration & dosage</subject><subject>Carrier Proteins - pharmacology</subject><subject>Cell Line, Tumor</subject><subject>Cetuximab</subject><subject>Doxorubicin - administration & dosage</subject><subject>Doxorubicin - pharmacology</subject><subject>Drug Delivery Systems</subject><subject>Drug Stability</subject><subject>Drug targeting</subject><subject>EGF receptor</subject><subject>Flow Cytometry</subject><subject>Folate</subject><subject>Folate binding protein</subject><subject>Folate Receptors, GPI-Anchored</subject><subject>Folic Acid</subject><subject>General pharmacology</subject><subject>Glioblastoma</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immunoconjugates - administration & dosage</subject><subject>Immunoconjugates - pharmacology</subject><subject>Immunoliposomes</subject><subject>Liposomes</subject><subject>Medical sciences</subject><subject>Microscopy, Fluorescence</subject><subject>Pharmaceutical technology. Pharmaceutical industry</subject><subject>Pharmacology. Drug treatments</subject><subject>Polycarboxylate Cement</subject><subject>Receptor, Epidermal Growth Factor - drug effects</subject><subject>Receptor, Epidermal Growth Factor - immunology</subject><subject>Receptor, Epidermal Growth Factor - metabolism</subject><subject>Receptors, Cell Surface - administration & dosage</subject><issn>0378-5173</issn><issn>1873-3476</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFu1DAQhi0EokvhEUC5wC1hbMexc0Jo1RakSkhVy9XyOmPwKrEX26nUW9-hb8iTkNVG6pHTzOH7Z359hLyn0FCg3ed94_eH3yZNDQPoGsoaAPmCbKiSvOat7F6SDXCpakElPyNvct7DAjLKX5MzKhllvaIb8nMbQy5ptsXHUEVXmVB8fXF1eVP5aZpDHP0h5jhhru69qVwcTcG_j0-npdr5MPjwqzqkWNCHyjjngy8Pb8krZ8aM79Z5Tu4uL2633-rrH1fft1-va8t7XmpUwgG3Sg6iVx20jvdAeQvKtQNYcEKYQQ20legkM8Jy2eFOoKOoAAT2_Jx8Ot1dCvyZMRc9-WxxHE3AOGctoe0YgyMoTqBNMeeETh-Sn0x60BT0Uaje61WoPgrVlOlF6JL7sD6YdxMOz6nV4AJ8XAGTrRldMsH6_MwpKVgvYeG-nDhcdNx7TDpbj8Hi4BPaoofo_1PlHzUymC8</recordid><startdate>20070524</startdate><enddate>20070524</enddate><creator>Pan, Xiaogang</creator><creator>Lee, Robert J.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</scope><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>20070524</creationdate><title>Construction of anti-EGFR immunoliposomes via folate–folate binding protein affinity</title><author>Pan, Xiaogang ; Lee, Robert J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-e85f03c87d598604f39013408f4d0c0f55ad8d147ef72a5c376eb5ef1e8005e93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Antibodies, Monoclonal - administration & dosage</topic><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Antibodies, Monoclonal, Humanized</topic><topic>Antineoplastic Agents - administration & dosage</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Biological Transport</topic><topic>Carrier Proteins - administration & dosage</topic><topic>Carrier Proteins - pharmacology</topic><topic>Cell Line, Tumor</topic><topic>Cetuximab</topic><topic>Doxorubicin - administration & dosage</topic><topic>Doxorubicin - pharmacology</topic><topic>Drug Delivery Systems</topic><topic>Drug Stability</topic><topic>Drug targeting</topic><topic>EGF receptor</topic><topic>Flow Cytometry</topic><topic>Folate</topic><topic>Folate binding protein</topic><topic>Folate Receptors, GPI-Anchored</topic><topic>Folic Acid</topic><topic>General pharmacology</topic><topic>Glioblastoma</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immunoconjugates - administration & dosage</topic><topic>Immunoconjugates - pharmacology</topic><topic>Immunoliposomes</topic><topic>Liposomes</topic><topic>Medical sciences</topic><topic>Microscopy, Fluorescence</topic><topic>Pharmaceutical technology. Pharmaceutical industry</topic><topic>Pharmacology. Drug treatments</topic><topic>Polycarboxylate Cement</topic><topic>Receptor, Epidermal Growth Factor - drug effects</topic><topic>Receptor, Epidermal Growth Factor - immunology</topic><topic>Receptor, Epidermal Growth Factor - metabolism</topic><topic>Receptors, Cell Surface - administration & dosage</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pan, Xiaogang</creatorcontrib><creatorcontrib>Lee, Robert J.</creatorcontrib><collection>Pascal-Francis</collection><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>International journal of pharmaceutics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pan, Xiaogang</au><au>Lee, Robert J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Construction of anti-EGFR immunoliposomes via folate–folate binding protein affinity</atitle><jtitle>International journal of pharmaceutics</jtitle><addtitle>Int J Pharm</addtitle><date>2007-05-24</date><risdate>2007</risdate><volume>336</volume><issue>2</issue><spage>276</spage><epage>283</epage><pages>276-283</pages><issn>0378-5173</issn><eissn>1873-3476</eissn><coden>IJPHDE</coden><abstract>A novel method for synthesis of anti-EGFR immunoliposomes using folate–folate binding protein (FBP) affinity is described. An anti-EGFR antibody (cetuximab or C225) was covalently linked to FBP via a thioether bond. Liposomes incorporating a lipophilic folate derivative (folate-PEG-cholesterol) were prepared by polycarbonate membrane extrusion. Anti-EGFR immunoliposomes were then obtained by combining FBP-C225 and folate-liposomes and evaluated for uptake and cytotoxicity in EGFR-overexpressing U87 human glioblastoma cells. Anti-EGFR immunoliposomes constructed via folate–FBP affinity exhibited excellent stability under physiological pH, and quickly released the bound FBP-C225 upon low pH (pH 3.5) treatment. Flow cytometry and fluorescence microscopy showed similar receptor-specific binding and internalization for both folate–FBP affinity-coupled and covalently coupled C225-immunoliposomes, but not for the non-targeted IgG-immunoliposomes. C225-immunoliposomes loaded with anticancer drug doxorubicin were more cytotoxic than non-targeted immunoliposomes in EGFR-overexpressing U87 glioma cells. Folate–FBP affinity is a potential method for construction of immunoliposomes and may have applications in synthesis of targeted drug carriers in general.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>17212981</pmid><doi>10.1016/j.ijpharm.2006.12.007</doi><tpages>8</tpages></addata></record> |
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| subjects | Antibodies, Monoclonal - administration & dosage Antibodies, Monoclonal - pharmacology Antibodies, Monoclonal, Humanized Antineoplastic Agents - administration & dosage Antineoplastic Agents - pharmacology Biological and medical sciences Biological Transport Carrier Proteins - administration & dosage Carrier Proteins - pharmacology Cell Line, Tumor Cetuximab Doxorubicin - administration & dosage Doxorubicin - pharmacology Drug Delivery Systems Drug Stability Drug targeting EGF receptor Flow Cytometry Folate Folate binding protein Folate Receptors, GPI-Anchored Folic Acid General pharmacology Glioblastoma Humans Hydrogen-Ion Concentration Immunoconjugates - administration & dosage Immunoconjugates - pharmacology Immunoliposomes Liposomes Medical sciences Microscopy, Fluorescence Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments Polycarboxylate Cement Receptor, Epidermal Growth Factor - drug effects Receptor, Epidermal Growth Factor - immunology Receptor, Epidermal Growth Factor - metabolism Receptors, Cell Surface - administration & dosage |
| title | Construction of anti-EGFR immunoliposomes via folate–folate binding protein affinity |
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