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Antibody-Hapten Recognition at the Surface of Functionalized Liposomes Studied by SPR: Steric Hindrance of Pegylated Phospholipids in Stealth Liposomes Prepared for Targeted Radionuclide Delivery.

Identifieur interne : 001593 ( Main/Exploration ); précédent : 001592; suivant : 001594

Antibody-Hapten Recognition at the Surface of Functionalized Liposomes Studied by SPR: Steric Hindrance of Pegylated Phospholipids in Stealth Liposomes Prepared for Targeted Radionuclide Delivery.

Auteurs : RBID : pubmed:21490749

Abstract

Targeted PEGylated liposomes could increase the amount of drugs or radionuclides delivered to tumor cells. They show favorable stability and pharmacokinetics, but steric hindrance of the PEG chains can block the binding of the targeting moiety. Here, specific interactions between an antihapten antibody (clone 734, specific for the DTPA-indium complex) and DTPA-indium-tagged liposomes were characterized by surface plasmon resonance (SPR). Non-PEGylated liposomes fused on CM5 chips whereas PEGylated liposomes did not. By contrast, both PEGylated and non-PEGylated liposomes attached to L1 chips without fusion. SPR binding kinetics showed that, in the absence of PEG, the antibody binds the hapten at the surface of lipid bilayers with the affinity of the soluble hapten. The incorporation of PEGylated lipids hinders antibody binding to extents depending on PEGylated lipid fraction and PEG molecular weight. SPR on immobilized liposomes thus appears as a useful technique to optimize formulations of liposomes for targeted therapy.

DOI: 10.1155/2011/368535
PubMed: 21490749

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<author><name sortKey="Botosoa, Eliot P" uniqKey="Botosoa E">Eliot P Botosoa</name>
<affiliation wicri:level="3"><nlm:affiliation>Centre de Recherche en Cancérologie Nantes-Angers (CRCNA), Université de Nantes, Inserm, UMR 892, Institut de Recherche Thérapeutique de l'Université de Nantes, 8 quai Moncousu, BP 70721, 44007 Nantes Cedex 1, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
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<author><name sortKey="Maillasson, Mike" uniqKey="Maillasson M">Mike Maillasson</name>
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<author><name sortKey="Mougin Degraef, Marie" uniqKey="Mougin Degraef M">Marie Mougin-Degraef</name>
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<author><name sortKey="Remaud Le Saec, Patricia" uniqKey="Remaud Le Saec P">Patricia Remaud-Le Saëc</name>
</author>
<author><name sortKey="Gestin, Jean Francois" uniqKey="Gestin J">Jean-François Gestin</name>
</author>
<author><name sortKey="Jacques, Yannick" uniqKey="Jacques Y">Yannick Jacques</name>
</author>
<author><name sortKey="Barbet, Jacques" uniqKey="Barbet J">Jacques Barbet</name>
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<author><name sortKey="Faivre Chauvet, Alain" uniqKey="Faivre Chauvet A">Alain Faivre-Chauvet</name>
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<front><div type="abstract" xml:lang="en">Targeted PEGylated liposomes could increase the amount of drugs or radionuclides delivered to tumor cells. They show favorable stability and pharmacokinetics, but steric hindrance of the PEG chains can block the binding of the targeting moiety. Here, specific interactions between an antihapten antibody (clone 734, specific for the DTPA-indium complex) and DTPA-indium-tagged liposomes were characterized by surface plasmon resonance (SPR). Non-PEGylated liposomes fused on CM5 chips whereas PEGylated liposomes did not. By contrast, both PEGylated and non-PEGylated liposomes attached to L1 chips without fusion. SPR binding kinetics showed that, in the absence of PEG, the antibody binds the hapten at the surface of lipid bilayers with the affinity of the soluble hapten. The incorporation of PEGylated lipids hinders antibody binding to extents depending on PEGylated lipid fraction and PEG molecular weight. SPR on immobilized liposomes thus appears as a useful technique to optimize formulations of liposomes for targeted therapy.</div>
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<Abstract><AbstractText>Targeted PEGylated liposomes could increase the amount of drugs or radionuclides delivered to tumor cells. They show favorable stability and pharmacokinetics, but steric hindrance of the PEG chains can block the binding of the targeting moiety. Here, specific interactions between an antihapten antibody (clone 734, specific for the DTPA-indium complex) and DTPA-indium-tagged liposomes were characterized by surface plasmon resonance (SPR). Non-PEGylated liposomes fused on CM5 chips whereas PEGylated liposomes did not. By contrast, both PEGylated and non-PEGylated liposomes attached to L1 chips without fusion. SPR binding kinetics showed that, in the absence of PEG, the antibody binds the hapten at the surface of lipid bilayers with the affinity of the soluble hapten. The incorporation of PEGylated lipids hinders antibody binding to extents depending on PEGylated lipid fraction and PEG molecular weight. SPR on immobilized liposomes thus appears as a useful technique to optimize formulations of liposomes for targeted therapy.</AbstractText>
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<Initials>EP</Initials>
<Affiliation>Centre de Recherche en Cancérologie Nantes-Angers (CRCNA), Université de Nantes, Inserm, UMR 892, Institut de Recherche Thérapeutique de l'Université de Nantes, 8 quai Moncousu, BP 70721, 44007 Nantes Cedex 1, France.</Affiliation>
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<CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Expert Opin Drug Deliv. 2010 Apr;7(4):461-78</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 1992 Jan 10;1103(1):94-100</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>J Mol Recognit. 2004 May-Jun;17(3):151-61</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>Anal Biochem. 2005 Sep 1;344(1):43-52</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>Chem Phys Lipids. 2006 Jun;141(1-2):169-78</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>Anal Bioanal Chem. 2006 Jun;385(3):433-51</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 1991 Feb 25;1062(2):142-8</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>J Drug Target. 2000;8(4):257-66</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>Methods Enzymol. 2003;372:99-124</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>Int J Pharm. 2007 Nov 1;344(1-2):110-7</RefSource>
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<CommentsCorrections RefType="Cites"><RefSource>J Mol Biol. 1965 Aug;13(1):238-52</RefSource>
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Antibody-Hapten Recognition at the Surface of Functionalized Liposomes Studied by SPR: Steric Hindrance of Pegylated Phospholipids in Stealth Liposomes Prepared for Targeted Radionuclide Delivery.

Antibody-Hapten Recognition at the Surface of Functionalized Liposomes Studied by SPR: Steric Hindrance of Pegylated Phospholipids in Stealth Liposomes Prepared for Targeted Radionuclide Delivery.

Abstract

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