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Influence of PEGylation and RGD loading on the targeting properties of radiolabeled liposomal nanoparticles.

Identifieur interne : 000C63 ( Main/Exploration ); précédent : 000C62; suivant : 000C64

Influence of PEGylation and RGD loading on the targeting properties of radiolabeled liposomal nanoparticles.

Auteurs : RBID : pubmed:23226020

English descriptors

Abstract

Liposomes have been proposed to be a means of selectively targeting cancer sites for diagnostic and therapeutic applications. The focus of this work was the evaluation of radiolabeled PEGylated liposomes derivatized with varying amounts of a cyclic arginyl-glycyl-aspartic acid (RGD) peptide. RGD peptides are known to bind to α(v)β(3) integrin receptors overexpressed during tumor-induced angiogenesis.

DOI: 10.2147/IJN.S36847
PubMed: 23226020

Links toward previous steps (curation, corpus...)


Le document en format XML

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<title xml:lang="en">Influence of PEGylation and RGD loading on the targeting properties of radiolabeled liposomal nanoparticles.</title>
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<name sortKey="Rangger, Christine" uniqKey="Rangger C">Christine Rangger</name>
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<nlm:affiliation>Department of Nuclear Medicine, Innsbruck Medical University, Austria.</nlm:affiliation>
<country xml:lang="fr">Autriche</country>
<wicri:regionArea>Department of Nuclear Medicine, Innsbruck Medical University</wicri:regionArea>
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<name sortKey="Helbok, Anna" uniqKey="Helbok A">Anna Helbok</name>
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<name sortKey="Von Guggenberg, Elisabeth" uniqKey="Von Guggenberg E">Elisabeth von Guggenberg</name>
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<name sortKey="Sosabowski, Jane" uniqKey="Sosabowski J">Jane Sosabowski</name>
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<author>
<name sortKey="Radolf, Thorsten" uniqKey="Radolf T">Thorsten Radolf</name>
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<name sortKey="Prassl, Ruth" uniqKey="Prassl R">Ruth Prassl</name>
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<author>
<name sortKey="Andreae, Fritz" uniqKey="Andreae F">Fritz Andreae</name>
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<name sortKey="Thurner, Gudrun C" uniqKey="Thurner G">Gudrun C Thurner</name>
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<name sortKey="Haubner, Roland" uniqKey="Haubner R">Roland Haubner</name>
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<name sortKey="Decristoforo, Clemens" uniqKey="Decristoforo C">Clemens Decristoforo</name>
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<front>
<div type="abstract" xml:lang="en">Liposomes have been proposed to be a means of selectively targeting cancer sites for diagnostic and therapeutic applications. The focus of this work was the evaluation of radiolabeled PEGylated liposomes derivatized with varying amounts of a cyclic arginyl-glycyl-aspartic acid (RGD) peptide. RGD peptides are known to bind to α(v)β(3) integrin receptors overexpressed during tumor-induced angiogenesis.</div>
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<Year>2012</Year>
<Month>12</Month>
<Day>11</Day>
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<DateCompleted>
<Year>2013</Year>
<Month>04</Month>
<Day>08</Day>
</DateCompleted>
<DateRevised>
<Year>2013</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
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<Journal>
<ISSN IssnType="Electronic">1178-2013</ISSN>
<JournalIssue CitedMedium="Internet">
<Volume>7</Volume>
<PubDate>
<Year>2012</Year>
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<Title>International journal of nanomedicine</Title>
<ISOAbbreviation>Int J Nanomedicine</ISOAbbreviation>
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<ArticleTitle>Influence of PEGylation and RGD loading on the targeting properties of radiolabeled liposomal nanoparticles.</ArticleTitle>
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<AbstractText Label="PURPOSE" NlmCategory="OBJECTIVE">Liposomes have been proposed to be a means of selectively targeting cancer sites for diagnostic and therapeutic applications. The focus of this work was the evaluation of radiolabeled PEGylated liposomes derivatized with varying amounts of a cyclic arginyl-glycyl-aspartic acid (RGD) peptide. RGD peptides are known to bind to α(v)β(3) integrin receptors overexpressed during tumor-induced angiogenesis.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">Several liposomal nanoparticles carrying the RGD peptide targeting sequence (RLPs) were synthesized using a combination of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, cholesterol, diethylenetriaminepentaacetic acid-derivatized lipids for radiolabeling, a polyethylene glycol (PEG) building block, and a lipid-based RGD building block. Relative amounts of RGD and PEG building blocks were varied. In vitro binding affinities were determined using isolated α(v)β(3) integrin receptors incubated with different concentrations of RLPs in competition with iodine-125-labeled cyclo-(-RGDyV-). Binding of the indium-111-labeled RLPs was also evaluated. Biodistribution and micro single photon emission computed tomography/computed tomography imaging studies were performed in nude mice using different tumor xenograft models.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">RLPs were labeled with indium-111 with high radiochemical yields. In vitro binding studies of RLPs with different RGD/PEG loading revealed good binding to isolated receptors, which was dependent on the extent of RGD and PEG loading. Binding increased with higher RGD loading, whereas reduced binding was found with higher PEG loading. Biodistribution showed increased circulating time for PEGylated RLPs, but no dependence on RGD loading. Both biodistribution and micro single photon emission computed tomography/computed tomography imaging studies revealed low, nonspecific tumor uptake values.</AbstractText>
<AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">In this study, RLPs for targeting angiogenesis were described. Even though good binding to α(v)β(3) integrin receptors was found in vitro, the balance between PEGylation and RGD loading clearly requires optimization to achieve targeting in vivo. These data form the basis for future development and provide a platform for the investigation of multimodal approaches.</AbstractText>
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<ForeName>Christine</ForeName>
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<Affiliation>Department of Nuclear Medicine, Innsbruck Medical University, Austria.</Affiliation>
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<Keyword MajorTopicYN="N">angiogenesis</Keyword>
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<Keyword MajorTopicYN="N">tumor targeting</Keyword>
<Keyword MajorTopicYN="N">αvβ3 integrin receptors</Keyword>
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