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university of tampere: faculty of medicine and life sciences: research:
Lääketieteen ja biotieteiden tiedekuntaUniversity of TampereLääketieteen ja biotieteiden tiedekunta
Vesa Hytönen - Protein Dynamics

About research group

Proteins adapt conformationally to their environment in response to chemical and physical signals arising from interactions with other molecules, and as a result of chemical modifications. Therefore, conformational changes in proteins are often essential for the protein function. The Protein Dynamics Group uses experimental and computational methods to elucidate the relation between protein conformation and function.

We study structural dynamics of the proteins in cellular adhesion sites called focal adhesions. In particular, we try to understand the mechanisms behind cellular mechanosensing. These studies involve cellular models, tailored hydrogel substrates for cell adhesion studies, protein engineering and molecular dynamics simulations. We collaborate in this project with University of Geneva.

Another approach to understand the impact of environment on protein conformation is a project where we study the effects of electric fields on protein structure and function. This research is performed in collaboration with University of Jyväskylä and Technical University of Tampere.

We utilize a broad set of biophysical characterization methods in our research, including calorimetry, biosensors and spectroscopic methods. Recombinant proteins and protein engineering are in routine use, and this expertise is utilized in research aiming for biofunctionalized materials, focusing on nanocellulose and various metals. In this field, we collaborate with VTT Espoo, University of Jyväskylä and Technical University of Tampere.

Our research group is also involved in projects developing novel diagnostic tools and vaccines. This work has a main focus on viruses, with the recently launched THERDIAB-project aiming to develop novel molecular tools to fight against enteroviral diseases and type 1 diabetes. This project is performed in collaboration with Karolinska Institutet.

Recent results

Stretching of talin rod

Using single-molecule atomic force microscopy (smAFM), we show that the entire talin rod can be unfolded by mechanical extension, over a physiological range of forces between 10 and 40 pN. We also demonstrate, through a combination of smAFM and steered molecular dynamics, that the different bundles within the talin rod exhibit a distinct hierarchy of mechanical stability. These results provide a mechanism by which different force conditions within the cell control a graduated unfolding of the talin rod. Mechanical unfolding of the rod subdomains, and the subsequent effect on talin's binding interactions, would allow for a finely tuned cellular response to internally or externally applied forces.

Haining et al.

All Subdomains of the Talin Rod Are Mechanically Vulnerable and May Contribute To Cellular Mechanosensing.

ACS Nano. 2016, 10(7), 6648-58.

Biofunctionalized antifouling stainless steel

Stainless steel was functionalized using heterobifunctional silane-polyethylene glycol overlayers. This resulted in reduced nonspecific biofouling of both proteins and bacteria. Furthermore, selective biofunctionalization of the modified surface were achieved by coupling biotinylated alkaline phosphatase to a silane-PEG-biotin overlayer via avidin-biotin bridges. The activity of the immobilized enzyme was shown to be well preserved without compromising the achieved antifouling properties. Overall, the simple solution-based approach enables the tailoring of SS to enhance its activity for biomedical and biotechnological applications.

Hynninen et al.

Improved antifouling properties and selective biofunctionalization of stainless steel by employing heterobifunctional silane-polyethylene glycol overlayers and avidin-biotin technology.

Sci. Rep. 2016, 6, 29324.

DNA electronics

Three gold nanoparticles were conjugated on a defined size TX-tile DNA assembly into a linear pattern to form nanometer scale isolated islands.  The conjugated structures were trapped using dielectrophoresis for current–voltage characterization. After trapping only high resistance behavior was observed. However, after extending the islands by chemical growth of gold, several structures exhibited Coulomb blockade behavior from 4.2 K up to room temperature, which gives a good indication that self-assembled DNA structures could be used for nanoelectronic patterning and single electron devices.

Tapio et al.

Towards single electron nanoelectronics using self-assembled DNA-structure.

Nano Lett. 2016

Press release:
Academy of Finland

Avidinylated electrospun nanofibers

Biotinylated bovine serum albumin was embedded into polylactic acid (PLA)-polyethylene glycol (PEG) fibers, which enabled specific immobilization of fluorescently labelled avidin. An alkaline phosphatase enzyme was immobilized via biotin-streptavidin interaction on the hybrid nanofibers, demonstrating the suitability of the material for biosensing applications.

Kumar et al.

Mixture of PLA-PEG and Biotinylated Albumin enables Immobilization of Avidins on Electrospun Fibers.

J. Biomed. Mater. Res. A. 2016

Previous results archive



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