Understanding the adsorption of proteins to surfaces is vital for biomaterial design and application. Protein coverage and conformation on surfaces has been shown to be determined by numerous factors, including surface chemistry, wettability, and nanoscale surface structure. Graphene is a material of increasing interest for biological applications due to its biocompatibility, remarkable electrical properties, and deformability. To date, there has been little study on the effects of graphene nanoscale structure on protein adsorption. Study of the effects of graphene surface roughness on the adsorption of immunoglobulin M (IgM) are described here. Graphene is mechanically deformed by shrinking of a thermoplastic substrate to form uniaxial wrinkles or random crumples. Contact angle measurements demonstrate the ability to tune the wettability of graphene by increasing the surface roughness. Atomic force microscopy (AFM) is used to map the IgM coverage on various graphene surfaces with nanometer resolution. Time-resolved protein adsorption behavior by AFM is also described. Additionally, progress towards single molecule measurements of IgM adhesion force to deformed graphene is included. Results suggest the ability to control protein coverage of graphene substrates through purely mechanical means, which is desirable for preserving the chemical and electrical properties of graphene. Additional control of protein coverage by arbitrary chemical patterning of graphene is also described.

Adsorption behavior of immunoglobulin M on mechanically deformed graphene

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.