How Do Proteins Associate with Nanoscale Metal–Organic Framework Surfaces?
Jacob Turner, Catherine J. Murphy
Abstract
It is well known that colloidal nanomaterials, upon exposure to a complex biological medium, acquire biomolecules on their surface to form coronas. Porous nanomaterials present an opportunity to sequester biomolecules and/or control their orientation at the surface. In this report, a metal-organic framework (MOF) shell around gold nanorods was compared to MOF nanocrystals as potential protein sponges to adsorb several common proteins (lysozyme, beta-lactoglobulin-A, and bovine serum albumin) and potentially control their orientation at the surface. Even after correction for surface area, MOF shell/gold nanorod materials adsorbed more protein than the analogous nanoMOFs. For the set of proteins and nanomaterials in this study, all protein-surface interactions were exothermic, as judged by isothermal titration calorimetry. Protein display at the surfaces was determined from limited proteolysis experiments, and it was found that protein orientation was dependent both on the nature of the nanoparticle surface and on the nature of the protein, with lysozyme and beta-lactoglobulin-A showing distinct molecular positioning.