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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

Novel avidin-based receptors for small molecules

Using phage display, several avidin forms, antidins, were developed capable of binding progesterone, hydrocortisone, testosterone, cholic acid, ketoprofen and folic acid, all with micromolar to nanomolar affinities. Importantly, the high thermal stability and characteristic structure of avidin were retained. Antidins may be used as an alternative to antibodies and are promising candidates for the development of novel diagnostics methods and other biomedical applications.

Lehtonen et al.

Artificial avidin-based receptors for a panel of small molecules

ACS Chem. Biol., 2016, 11 (1), pp 211–221

http://pubs.acs.org/doi/10.1021/acschembio.5b00906

SERS detection of cell surface and intracellular components of microorganisms using nano-aggregated Ag substrate

Tibebe Lemma, Alex Saliniemi, Ville Hynninen, Vesa P. Hytönen, J. Jussi Toppari

The intracellular and extracellular components of bacteria were investigated using SERS. A comparison of the spectra of gram positive and negative bacteria revealed significant differences between their Raman spectra. Moreover, distinct features were observed in between lysed and nontreated cells, which reflects the availability of the chemical structures to nanoparticle-enhanced electric field. This study illustrates the potential of SERS in the detection and identification of bacterial components.

http://www.sciencedirect.com/science/article/pii/S0924203116300066

doi:10.1016/j.vibspec.2016.01.006

Regenerative biosensor chips based on switchable mutants of avidin-A systematic study

A series of avidin mutants were found to be suitable for reversible immobilization of biotinylated baits on biotinylated sensor chips. The stably formed biotin-avidin-biotin bridges can be quantitatively dissolved when desired. This methodology enables chip recycling in biosensing research.

Dominik Zauner, Barbara Taskinen, Daniel Eichinger, Clemens Flattinger, Bianca Ruttmann, Claudia Knoglinger, Lukas Traxler, Andreas Ebner, Hermann J. Gruber, Vesa P. Hytönen

Sensors and Actuators B: Chemical, 229, 646-654
http://www.sciencedirect.com/science/article/pii/S0925400516301885

Horizontal transfer of β-carbonic anhydrase genes

Horizontal gene transfer (HGT) refers to movement of DNA across mating barriers to less phylogenetically distinct organisms. Several eukaryotes, including protozoans contain prokaryotic endosymbionts. Using different prediction and modelling techniques, we identified 40 Mobile Genetic Elements (MGEs) containing transposase, integrase, and resolvase, which give the ability to prokaryotes to transfer their β-carbonic anhydrase genes to their protozoan, insect, and nematode hosts.

Reza Zolfaghari Emameh, Harlan R. Barker, Martti E.E. Tolvanen, Seppo Parkkila, Vesa P. Hytönen

Horizontal transfer of β-carbonic anhydrase genes from prokaryotes to protozoans, insects and nematodes. Parasites & Vectors 9, 152.

http://parasitesandvectors.biomedcentral.com/articles/10.1186/s13071-016-1415-7

Previous results archive

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Last update: 18.3.2016 14.42 Muokkaa

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