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Design, Construction, and Characterization of High-Performance Membrane Fusion Devices with Target-Selectivity.
MedLine Citation:
PMID:  22204500     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Membrane fusion proteins such as the hemagglutinin glycoprotein have target recognition and fusion accelerative domains, where some synergistically working elements are essential for target-selective and highly effective native membrane fusion systems. In this work, novel membrane fusion devices bearing such domains were designed and constructed. We selected a phenylboronic acid derivative as a recognition domain for a sugar-like target and a transmembrane-peptide (Leu-Ala sequence) domain interacting with the target membrane and accelerating the fusion process. Artificial membrane fusion behavior between the synthetic devices in which pilot and target liposomes were incorporated was characterized by lipid-mixing and inner-leaflet lipid-mixing assays. In consequence, the devices bearing both of the recognition and transmembrane domains brought about a remarkable increase in the initial rate for the membrane fusion compared with the devices containing the recognition domain alone. In addition, a weakly acidic pH-responsive device was also constructed by replacing three Leu residues in the transmembrane-peptide domain by Glu residues. The presence of Glu residues made the acidic pH-dependent hydrophobic alpha-helix formation possible as expected. The target-selective liposome-liposome fusion was accelerated in a weakly acidic pH range when the Glu-substituted device was incorporated in pilot liposomes. The using of this pH-responsive device seems to be a potentially strategy for novel applications in a liposome-based delivery system.
Authors:
Ayumi Kashiwada; Iori Yamane; Mana Tsuboi; Shun Ando; Kiyomi Matsuda
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-12-28
Journal Detail:
Title:  Langmuir : the ACS journal of surfaces and colloids     Volume:  -     ISSN:  1520-5827     ISO Abbreviation:  -     Publication Date:  2011 Dec 
Date Detail:
Created Date:  2011-12-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882736     Medline TA:  Langmuir     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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