Adenovirus knob trimers as tailorable scaffolds for nanoscale assembly

The use of proteins derived from Adenovirus, whose knob fragments trimeric structure and relative small size allow its use as the multidentate assembly agent with gold nanoparticles, was described. The mutant proteins were expressed in E. Coli and shown by gel electrolysis to assemble into SDS-resistance trimeric quaternary conformations. The DLS results suggest a relative polydisperse aggregate population, which is also manifested in loss SP-band extinction, due to increased scattering components and screened Au dilution extinction. The unique phenomena of the knob-1 system revealed an isolated nanoparticle phase, which consist of only knob-1 encapsulated Au. The nonmonotonic dependence of knob-Au assembly on concentration ratios is determined by the competition between the knob's mono and trivalent binding, which depends on the number of available sites on the nanoparticles.