Patterning of Ferritin Nanoparticles on Gold Posts of Silicon Substrate

ORAL

Abstract

Patterning and immobilizing protein nanoparticles with nanometer-scale control has been proven integral to a range of applications in the development of biochip arrays, biosensor and electronic devices. Protein nanoparticles, such as ferritin nanoparticles, have a uniform size distribution and shape that can be used to construct well-defined patterns with nanoscale features. Here, the gold posts on silicon were produced using block copolymer PS (47.6 kg/mol)-b-P4VP (20.9 kg/mol) (PDI: 1.14) as a template and then gold chloride solution~was loaded into P4VP domain. After reducing gold salt into gold and removing the block copolymer using anoxygen plasma, producing a pattern of gold posts. Thiol modified horse spleen ferritin are anchored to gold posts of silicon substrate by the binding of thiol and gold. Scanning electron microscopy (SEM) shows that the feature size of gold posts decreased from 30 nm to 13 nm after attached with modified ferritin nanoparticles, which is consistent with size of modified ferritin. Also XPS result shows nitrogen and ion elements on ferritin-attached gold posts, and the signal of gold was attenuated after ferritin attached.

Authors

  • Yunxia Hu

    Dept. of Polymer Science and Engineering, University of Massachusetts Amherst

  • Dian Chen

    Dept. of Polymer Science and Engineering, University of Massachusetts Amherst

  • Soojin Park

    Dept. of Polymer Science and Engineering, University of Massachusetts Amherst

  • Todd Emrick

    Dept. of Polymer Science and Engineering, University of Massachusetts Amherst, Dept. of Polymer Sciece and Engineering, UMass Amherst

  • Thomas Russell

    Dept. of Polymer Science and Engineering, University of Massachusetts Amherst, Department of Polymer Science and Engineering, University of Massachusetts-Amherst, University of Massachusetts, University of Massachusetts, Amherst, PSE,UMASS Amherst, Univ of Massachusetts Amherst, Univ of Massachusetts, Amherst, University of Massachusetts Amherst