Abstract:
:Understanding the self-assembly mechanism of caged proteins provides clues to develop their potential applications in nanotechnology, such as a nanoscale drug delivery system. The E2 protein from Bacillus stearothermophilus , with a virus-like caged structure, has drawn much attention for its potential application as a nanocapsule. To investigate its self-assembly process from subunits to a spherical protein cage, we truncate the C-terminus of the E2 subunit. The redesigned protein subunit shows dynamic transition between monomer and trimer, but not the integrate 60-mer. The results indicate the role of the trimer as the intermediate and building block during the self-assembly of the E2 protein cage. In combination with the molecular dynamics simulations results, we conclude that the C-terminus modulates the self-assembly of the E2 protein cage from trimer to 60-mer. This investigation elucidates the role of the intersubunit interactions in engineering other functionalities in other caged structure proteins.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Peng T,Lee H,Lim Sdoi
10.1021/bm201587qsubject
Has Abstractpub_date
2012-03-12 00:00:00pages
699-705issue
3eissn
1525-7797issn
1526-4602journal_volume
13pub_type
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