Using sophisticated microscopy techniques, researchers show why proteins stick better to some surfaces than others. The details could be important to manufacturers fine-tuning drug purifications, biosensors or anti-fouling surfaces.

Exactly how proteins interact with solid surfaces is a concern for health care manufacturers who design drugs, make biosensors or develop anti-fouling materials.

The mechanisms that control these interactions are hard to see, but researchers at Rice University are changing that with a microscopy technique to assess the effects of surface roughness as well as water-repelling properties (hydrophobicity) and electrostatic charge. The ability to tune those parameters will lead to more predictable materials.

«The main idea is to understand the how the combination of these properties influences protein dynamics,» said Anastasiia Misiura, lead author of a study in the Journal of Chemical Physics and a graduate student in the Rice lab of chemist Christy Landes. «It turned out that roughness and hydrophobicity are opposite forces, but proteins get stuck on areas that are very rough.»

The paper, an «editor’s choice,» is part of the journal’s «Ever-Expanding Optics of Single Molecules and Nanoparticles» collection.

How molecules interact at surfaces is important at every scale in the physical realm, from grinding planetary plates to brakes grabbing the wheels in your car to the invisible molecular transactions that make life possible. Understanding these mechanisms at the very smallest level is the focus of Landes’ lab as its members attempt to clarify what’s actually happening down there.

Story Source:
Materials provided by Rice University. Original written by Mike Williams. Note: Content may be edited for style and length.