Nanoscale protein patterning using self-assembled diblock copolymers.
Novel methods for immobilizing proteins on surfaces have the potential to impact basic biological research as well as various biochip applications. Here, we demonstrate a unique method to pattern proteins with a nanometer periodicity on silicon oxide substrates using microphase-separated diblock copolymer thin films. We developed a straightforward and effective protein immobilization technique using the microphase-separated domains of polystyrene-block-poly(methyl methacrylate) to localize various model protein molecules such as bovine immunoglobulin G, fluorescein isothiocyanate conjugated anti-bovine immunoglobulin G, and protein G. The self-organizing nature of the diblock copolymer was exploited to produce periodically alternating, nanometer-spaced polymeric domains exposing the two chemical compositions of the diblock to surface. We demonstrate that the model proteins selectively self-organize themselves on the microdomain regions of specific polymer components due to their preferential interactions with one of the two polymer segments. This diblock copolymer-based, self-assembly approach represents a step forward for facile, nanometer-spaced protein immobilization with high areal density and could provide a pathway to high-throughput proteomic arrays and biosensors.
Kumar
Nitin
N
Department of Chemical Engineering, Pennsylvania State University, 160 Fenske Laboratory, University Park, Pennsylvania 16802, USA.
Hahm
Jong-in
JI
D018625:Microscopy, Atomic Force; D036103:Nanotechnology; D019904:Polymethyl Methacrylate / Q000737:chemistry*; D011137:Polystyrenes / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*
D011137:Polystyrenes; D011506:Proteins; D019904:Polymethyl Methacrylate