TY - JOUR
T1 - How Do Proteins Associate with Nanoscale Metal-Organic Framework Surfaces?
AU - Turner, Jacob G.
AU - Murphy, Catherine J.
N1 - Funding Information:
We thank the National Science Foundation for its support of this work under CHE-1608743. Protein fragmentation mass spectrometry analysis was done by the Roy J. Carver Biotechnology Center, University of Illinois at Urbana-Champaign. XRD was performed in the George L. Clark X-Ray Facility and 3M Materials Laboratory, School of Chemical Sciences, University of Illinois at Urbana-Champaign. ITC and N adsorption measurements were conducted at the Microanalysis Laboratory, School of Chemical Sciences, University of Illinois at Urbana-Champaign. Electron microscopy was done at the Frederick Seitz Materials Research Laboratory Central Research Facilities, University of Illinois at Urbana-Champaign. The Table of Contents graphic was created using BioRender. 2
Publisher Copyright:
© 2021 American Chemical Society.
PY - 2021/8/3
Y1 - 2021/8/3
N2 - 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.
AB - 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.
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U2 - 10.1021/acs.langmuir.1c01664
DO - 10.1021/acs.langmuir.1c01664
M3 - Article
C2 - 34343005
AN - SCOPUS:85113413439
SN - 0743-7463
VL - 37
SP - 9910
EP - 9919
JO - Langmuir
JF - Langmuir
IS - 32
ER -