Abstract:
:We demonstrate the fabrication of protein·gold nanoparticle (AuNP) nanocomposites in situ, leading to distinct assemblies dependent upon protein secondary structure. In the presence of pentameric coiled-coil proteins C and Q, which contain histidine tags and have helicities of 54 and 65%, respectively, templation of AuNP results in precipitation of the protein·AuNP composites with AuNPs 6.5 nm in diameter, creating macromolecular assemblies on the micrometer scale. In the absence of the histidine tags, the resulting Cx and Qx proteins, which exhibit lower helicities of 37 and 45%, respectively, stabilize soluble protein·AuNP composites with AuNPs 4.5 nm in diameter for several days without aggregating. By manipulating protein structure via external triggers, such as TFE, we obtain control over the macromolecular conformation and overall physicochemical properties. These hybrid protein·AuNP assemblies can be readily deposited on electrodes, where they can serve as a tunable bionanocomposite kinetic barrier.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Hume J,Chen R,Jacquet R,Yang M,Montclare JKdoi
10.1021/acs.biomac.5b00098subject
Has Abstractpub_date
2015-06-08 00:00:00pages
1706-13issue
6eissn
1525-7797issn
1526-4602journal_volume
16pub_type
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