How Do Proteins Associate with Nanoscale Metal-Organic Framework Surfaces?

Area of Science:

• Nanomaterials Science
• Biomaterials Engineering
• Surface Chemistry

Background:

• Colloidal nanomaterials acquire biomolecular coronas in biological media.
• Porous nanomaterials can sequester and orient biomolecules on their surfaces.

Purpose of the Study:

• To compare MOF-shelled gold nanorods with MOF nanocrystals as protein adsorbents.
• To investigate the control of protein orientation on these nanomaterials.

Main Methods:

• Adsorption of lysozyme, beta-lactoglobulin-A, and bovine serum albumin.
• Isothermal titration calorimetry to determine interaction thermodynamics.
• Limited proteolysis to assess protein surface display and orientation.

Main Results:

• MOF-shelled gold nanorods adsorbed more protein than MOF nanocrystals, even after surface area correction.
• All protein-surface interactions were exothermic.
• Protein orientation was dependent on both the nanoparticle surface and the specific protein.

Conclusions:

• MOF-shelled gold nanorods demonstrate enhanced protein adsorption capacity.
• Protein orientation on nanomaterial surfaces is a complex, protein- and surface-specific phenomenon.
• These findings advance the understanding of biomolecule-nanoparticle interactions for applications in biosensing and drug delivery.