Abstract:
:The single-coat protein (CP) of bacteriophage Qβ self-assembles into T = 3 icosahedral virus-like particles (VLPs), of interest for a wide range of applications. These VLPs are very stable, but identification of the specific molecular determinants of this stability is lacking. To investigate these determinants along with manipulations that confer more capabilities to our VLP material, we manipulated the CP primary structure to test the importance of various putative stabilizing interactions. Optimization of a procedure to incorporate fused CP subunits allowed for good control over the average number of covalent dimers in each VLP. We confirmed that the disulfide linkages are the most important stabilizing elements for the capsid and that acidic conditions significantly enhance the resistance of VLPs to thermal degradation. Interdimer interactions were found to be less important for VLP assembly than intradimer interactions. Finally, a single point mutation in the CP resulted in a population of smaller VLPs in three distinct structural forms.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Fiedler JD,Higginson C,Hovlid ML,Kislukhin AA,Castillejos A,Manzenrieder F,Campbell MG,Voss NR,Potter CS,Carragher B,Finn MGdoi
10.1021/bm300590xsubject
Has Abstractpub_date
2012-08-13 00:00:00pages
2339-48issue
8eissn
1525-7797issn
1526-4602journal_volume
13pub_type
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