Elucidating Fundamental Factors Driving Self-assembly with Guided Interactions in Multicomponent Enzyme Systems Using Model Nanostructured Platforms

With the support of the Macromolecular, Supramolecular and Nanochemistry program in the Division of Chemistry and the Established Program to Stimulate Competitive Research (EPSCoR), Professors Cindy L. Berrie and Candan Tamerler at the University of Kansas are investigating factors that govern the assembly and organization of biomolecules at interfaces.

Affinity peptide tags will be used to selectively direct the self-assembly of biomolecules, including enzymes, onto material surfaces to create multicomponent bioactive materials organized at the nanoscale. The metal nanostructure platforms being developed are designed to enable an understanding of the role of material specificity, curvature, spacing, and size on the spatially organized self-assembly of biomolecules.

The project will allow biohybrid materials to mimic the exquisite functionality nature has evolved for complex tasks, which will enable enhanced biosensing, biocatalysis and biofuel applications as an alternative energy source. In the course of conducting the project, graduate and undergraduate students will be trained in the growing convergence of nanoscience, biomolecules and biomaterials.

In addition, the research team will carry out outreach and services to the community at the University of Kansas and local middle and elementary schools through participation in the Engineering EXPO and the Carnival of Chemistry events and the development of the “Science Night” program to engage students in science at an early stage. Public demonstrations on nanolithography and imaging will be conducted with the involvement of the students working on the project.

The project focuses on exploring the fundamental factors responsible for peptide guided self-assembly of multi-enzyme systems using model nanostructured platforms to harness their coordinated activity. Nature exquisitely organizes cascades of enzymes to work in tandem; however, attempts to artificially assemble such complex systems are hampered by the complexity and lack of information about the factors governing functional assembly.

Emerging applications from biocatalysis to biosensing, to energy harvesting and biofuels would likely benefit from assembly of coupled enzymes with cascade-like activity, and therefore elucidating the factors controlling the assembly of such complex systems would have wide ranging applications. Specifically, the assembly of peptide tags, peptide-labeled enzymes, and the co-assembly of coupled enzyme pairs will be investigated using optical and atomic force microscopy as well as bioactivity assays to determine the distribution, conformation, and orientation of assembled biomolecules and how these are affected by the metal nanostructure composition, spacing, size, and curvature.

The scientific broader impacts of the work include the development of design principles for biohybrid materials for applications in biosensing and biocatalysis. There are also important elements of workforce development in the area of nanobiomaterials and of outreach the community.

This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.