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      Liposomes bi-functionalized with phosphatidic acid and an ApoE-derived peptide affect Aβ aggregation features and cross the blood-brain-barrier: implications for therapy of Alzheimer disease.

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          Abstract

          Targeting amyloid-β peptide (Aβ) within the brain is a strategy actively sought for therapy of Alzheimer's disease (AD). We investigated the ability of liposomes bi-functionalized with phosphatidic acid and with a modified ApoE-derived peptide (mApoE-PA-LIP) to affect Aβ aggregation/disaggregation features and to cross in vitro and in vivo the blood-brain barrier (BBB). Surface plasmon resonance showed that bi-functionalized liposomes strongly bind Aβ (kD=0.6 μM), while Thioflavin-T and SDS-PAGE/WB assays show that liposomes inhibit peptide aggregation (70% inhibition after 72 h) and trigger the disaggregation of preformed aggregates (60% decrease after 120 h incubation). Moreover, experiments with dually radiolabelled LIP suggest that bi-functionalization enhances the passage of radioactivity across the BBB either in vitro (permeability=2.5×10(-5) cm/min, 5-fold higher with respect to mono-functionalized liposomes) or in vivo in healthy mice. Taken together, our results suggest that mApoE-PA-LIP are valuable nanodevices with a potential applicability in vivo for the treatment of AD. From the clinical editor: Bi-functionalized liposomes with phosphatidic acid and a modified ApoE-derived peptide were demonstrated to influence Aβ aggregation/disaggregation as a potential treatment in an Alzheimer's model. The liposomes were able to cross the blood-brain barrier in vitro and in vivo. Similar liposomes may become clinically valuable nanodevices with a potential applicability for the treatment of Alzheimer's disease.

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          Author and article information

          Journal
          Nanomedicine
          Nanomedicine : nanotechnology, biology, and medicine
          Elsevier BV
          1549-9642
          1549-9634
          Oct 2014
          : 10
          : 7
          Affiliations
          [1 ] Department of Health Sciences, University of Milano-Bicocca, Monza, Italy.
          [2 ] Department of Biochemistry and Molecular Pharmacology, Mario Negri Institute for Pharmacological Research IRCCS, Milano, Italy.
          [3 ] Department of Genome Analysis, Academic Medical Center, Amsterdam, AZ, The Netherlands.
          [4 ] Department of Genome Analysis, Academic Medical Center, Amsterdam, AZ, The Netherlands; Department of Neurology, Academic Medical Center, Amsterdam, AZ, The Netherlands.
          [5 ] Department of Health Sciences, University of Milano-Bicocca, Monza, Italy. Electronic address: massimo.masserini@unimib.it.
          Article
          S1549-9634(13)00684-9
          10.1016/j.nano.2013.12.001
          24333591

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