This talk presents our on-going research aiming to provide fundamental understanding on nanoscale protein adsorption behaviors uniquely observed on diblock copolymer (BCP) nanodomains. In a series of studies, we have systematically examined a range of nanoscale polymeric materials that exhibit varying degrees of chemical heterogeneity, periodicity, and alignment in their phase-separated domains. Intriguing protein adsorption phenomena on these surfaces were then directly probed at the individual biomolecule level via high-resolution imaging.<br/>We have elucidated distinctive adsorption and assembly characteristics of globular and elongated proteins on various polystyrene-block-polymethylmethacrylate (PS-b-PMMA) and polystyrene-block-polyvinylpyridine (PS-b-PVP) templates. This presentation outlines the key results from these studies. The effects of chemical interfaces, domain size, domain orientation presented by each BCP template on the adsorption behaviors of the different protein types will be discussed. The roles played by the different types of proteins on the same BCP surface will be also explained. Our results demonstrate that self-assembling, chemically alternating, nanoscale BCP materials can be effectively used for conveniently creating well-defined, biofunctional, 2D protein arrays. Insight gained from our findings may be used to control the dimension, density, conformation, orientation, and biofunctionality of surface-bound proteins. Our overall approach can be particularly beneficial since the fabrication of periodically patterned proteins on BCP surfaces into nanoscopic dimensions can be facilely attained without the use of electron beam or extreme UV lithography and without the need for an external electric or shear field. Therefore, our approach will have important implications in highly miniaturized proteomic detection and biosensing.

Surface assembly configurations and packing preferences of various proteins on block copolymer nanodomains

256th National Meeting (2018)

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