Interfaces play a deciding role in many aspects of modern chemistry and material science – catalysis, adhesion, sensing, nucleation are all processes driven by interfaces.
We use methods based on static and time-resolved sum frequency generation to probe the orientation, structure and dynamics of molecules at interfaces. Near-edge X-ray absorption fine structure (NEXAFS) spectroscopy and microscopy are used as complementary tools to probe binding chemistry, surface distribution and molecular structure.
An important part of our research are protein structures at interfaces. Specific proteins can act as Nature’s engineers of both hard and soft tissue. Proteins can ‘sculpture’ biogenic minerals and shape cell membranes. The control interfacial proteins exert over biological surfaces has relevance for disciplines as diverse as cell biology, bio-sensor research, biomimetics and material science. We ask how proteins fold and move at surfaces and how energy flows through protein interfaces.
For technical applications we use chemical modification of surfaces to prevent biofouling and scaling and to reduce friction. The approaches we use are inspired by our studies of the surface chemistry of animals. Can we fabricate self-cleaning surfaces like plants? Stick to walls like a spider? Glue like a frog tongue?
The goal of our research is to understand how molecules operate at surfaces and how we can control interfacial processes at the molecular level.
March 2022 - Paper in the Journal of Physical Chemistry Letters
Katinka Holler, Mette Rasmussen, and Tobias Weidner have published a paper about the structure of proteins in gecko feet.
December 2021 - Article in Biomacromolecules
Surflab researchers, together with collaborators from the Department of Molecular Biology and Genetics at Aarhus University, have published an article in Biomacromolecules entitled "Electrostatics Trigger Interfacial Self-Assembly of Bacterial Ice Nucleators".
Link to the article: https://doi.org/10.1021/acs.biomac.1c01217
Surflab researchers and a team of collaborators have published an article in Langmuir entitled "Membrane Structure of Aquaporin Observed with Combined Experimental and Theoretical Sum Frequency Generation Spectroscopy".
The work highlights the protein structure sensitivity of SFG spectroscopy.