Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/55159
Type: Artigo de periódico
Title: Attachment of water-soluble proteins to the surface of (magnetizable) phospholipid colloids via NeutrAvidin-derivatized phospholipids
Author: De Cuyper, M
Hodenius, M
Lacava, ZGM
Azevedo, RB
da Silva, MD
Morais, PC
Santana, MHA
Abstract: The present work describes the incorporation of a functionalized phospholipid derivative into the phospholipid bilayer of both classical small unilamellar vesicles and recently developed magnetoliposomes, resulting in unique biocolloid structures onto which peripheral water-soluble enzymes can be immobilized on the surfaces. In the first part of this work, a synthesis protocol is outlined for a universal membrane anchor for water-soluble proteins. Dioleoylphosphatidylethanolamine-N-dodecanyl was used as the starting lipid molecule. After activation of the terminal -COOH group, alpha,omega-diamino-poly(ethylene glycol), used as a hydrophilic, flexible spacer arm, was coupled covalently. Subsequently, NeutrAvidin was bound, after blocking the free -NH2 groups with citraconic anhydride. In the second part, the resulting lipid-NeutrAvidin derivative was incorporated into small unilamellar vesicles comprised of dimyristoylphosphatidylglycerol. FPLC with Superdex 200 as the column matrix clearly showed that biotinylated alkaline phosphatase, which served as a representative model of water-soluble proteins, was attached to the vesicles. Furthermore, magnetoliposomes, constructed of the same type of phospholipid molecules, were presented as interesting colloids to assess the degree of enzyme immobilization in a rapid and elegant manner. Potential applications that can emerge from this study are briefly discussed. (C) 2002 Elsevier Science.
Subject: magnetoliposomes
NeutrAvidin
phospholipid-polymer complexes
phospholipid vesicles
protein immobilization
Stealth liposomes
sterically stabilized (magneto)liposomes
Country: EUA
Editor: Academic Press Inc Elsevier Science
Rights: fechado
Identifier DOI: 10.1006/jcis.2001.8043
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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