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Issue 1, 2013
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Self assembly and pore formation of HIV GP160 revealed at molecular resolution

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Abstract

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.

Graphical abstract: Self assembly and pore formation of HIV GP160 revealed at molecular resolution

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Publication details

The article was received on 26 Aug 2012, accepted on 09 Oct 2012 and first published on 18 Oct 2012


Article type: Paper
DOI: 10.1039/C2SM26980E
Citation: Soft Matter, 2013,9, 283-290
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    Self assembly and pore formation of HIV GP160 revealed at molecular resolution

    L. Donlon and D. Frankel, Soft Matter, 2013, 9, 283
    DOI: 10.1039/C2SM26980E

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