Metal-Organic Framework Preserves the Biorecognition of Antibodies on Nanoscale Surfaces Validated by Single-Molecule Force Spectroscopy.

Antibody biorecognition forms the basis for numerous biomedical applications such as diagnostic assays, targeted drug delivery, and targeted cancer imaging. However, antibodies, especially after being conjugated to surfaces or nanostructures, suffer from stability issues when stored under nonrefrigeration conditions. Therefore, enhancing the stability of antibodies on surfaces and nanostructures under ambient and elevated temperatures is of paramount importance for many nanobiotechnology applications. In this study, we introduce a simple and facile approach based on a metal-organic framework (MOF) coating to preserve the biorecognition capability of antibodies immobilized on nanoscale surfaces after exposure to elevated temperatures for a prolonged period. By using atomic force microscopy (AFM)-based force spectroscopy, we demonstrate that the MOF coating is able to preserve the binding force and binding frequency of the anti-CD-146 antibody attached to an AFM tip to CD-146 antigen on the surface of melanoma cells at the single-molecule level. We also demonstrate that the MOF coating outperforms another commonly used sucrose coatings in terms of maintaining the binding force and binding frequency of the antibody to antigen. Herein, the AFM tip functionalized with antibodies provides a nanoscale testbed (analogous to an antibody-conjugated nanostructure) to assess antibody biorecognition at the single-molecule level and preservation efficacy under antibody denaturing conditions. This MOF coating approach should be applicable to the preservation of a variety of antibody-conjugated nanostructures aiming for targeted drug delivery, targeted cancer imaging, and nanobiosensors. The improved stability and elimination of refrigeration requirements will facilitate wide applications of antibody-enabled nanobiotechnology in resource-limited environments and populations.