Lookup NU author(s): Dr Lynn Donlon,
Dr Daniel Frankel
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Protein assembly at interfaces is fundamental to disease pathology and biological function. Here we report on the self assembly of the HIV viral envelope protein HIV GP160 and its interaction with phospholipids. The protein can assemble to form either pores or large aggregates. The process of aggregation can be observed at molecular resolution giving a rare insight into the assembly process. HIV GP160 was reconstituted into lipid bilayers simulating the HIV viral envelope and exhibited similar self assembly behaviour to the naked protein. When HIV GP160 was adsorbed on top of a pure single phase phospholipid bilayer it gradually "sank in" over time. Such a variety of self assembly modes and lipid interactions could be critical to the behaviour of the protein in the viral envelope and subsequent viral infection.
Author(s): Donlon L, Frankel D
Publication type: Article
Publication status: Published
Journal: Soft Matter
Print publication date: 18/10/2012
ISSN (print): 1744-683X
ISSN (electronic): 1744-6848
Publisher: RSC Publications
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