Bottom-up Protein Assembly at Nanoscale: Towards High Density, High Payload, Quantifiable Protein Arrays

Friday, May 4, 2012 – 12:00pm
Reiss 261A
Jong-in Hahm
Department of Chemistry, Georgetown University

We evaluate protein adsorption characteristics on chemically homogeneous and
heterogeneous polymeric surfaces by employing diblock copolymers, homopolymers, and polymer blends as protein templates. We also carry out for the first time quantitative activity measurements of various enzymes immobilized selectively on one of the domains in microphase-separated block copolymer films. The specific activity of enzymes adsorbed on the diblock copolymer surface are measured and compared quantitatively to that of enzymes in free solution. Protein assembly on chemically modified polymeric nanotemplates is also explored in order to demonstrate the versatility of our new methods in providing different template sizes and shapes. Our results demonstrate that a wide range of self-assembling, chemically heterogeneous, nanoscale domains in diblock copolymers can be used as basis for extremely high density protein arrays. Subsequently, the resulting protein nanoarrays can serve as novel, high density, high payload, biologically functional platforms in many proteomics applications.