- Keywords: Amyloid, prion, protein aggregation, protein misfolding, proteinaceous infectivity, neurodegenerative diseases
The group studies effects of environmental factors such as temperature, pressure, pH, prions, macromolecular crowding, and the presence of different organic solvents, ligands and biomolecules on aggregation kinetics, thermodynamic stability, and structural properties of amyloid-like fibrils. We believe that only comprehensive knowledge of all factors may give genuine understanding of mechanisms of amyloid self-replications and thus proteinaceous infectivity.
Research group activities
Protein aggregation into amyloid structure has been associated with many human diseases, including such neurodegenerative disorders as Alzheimer’s and Parkinson’s, systemic amyloidosis and even some localized diseases such as type II diabetes or cataracts. There is an increasing evidence of amyloid nature of proteinaceous infectious particles – prions. One of possible ways of prion spreading is self-replication of amyloid-like fibrils, thus there is a chance of all amyloid-associated diseases to be potentially infective. We study effects of environmental factors such as temperature,pH, macromolecular crowding, prions,pressure and the presence of different organic solvents, ligands and biomolecules on aggregation kinetics, thermodynamic stability, and structural properties of amyloid-like fibrils. We believe that only comprehensive knowledge of all factors may give genuine understanding of mechanisms of amyloid self-replications and thus proteinaceous infectivity.
- We offer expertise in studies of protein misfolding and aggregation and in production of recombinant amyloid-related proteins.
- We are open for collaborative projects related to protein misfolding and aggregation.
- We are looking for partners for developing competitive research projects targeting HORIZON 2020 and other international programs.
Meet our team
Dr. Vytautas Smirnovas
Undergraduate and postgraduate students
Mai Nguyen Ngoc
- Iashchishyn, I. A., Sulskis, D., Nguyen Ngoc, M., Smirnovas, V. & Morozova-Roche, L. A. Finke–Watzky Two-Step Nucleation–Autocatalysis Model of S100A9 Amyloid Formation: Protein Misfolding as ‘Nucleation’ Event. ACS Chemical Neuroscience 8, 2152–2158 (2017).
- Šneideris T, Baranauskienė L, Cannon JG, Rutkienė R, Meškys R, Smirnovas V (2015) Looking for a generic inhibitor of amyloid-like fibril formation among flavone derivatives. PeerJ 3:e1271.
- Sneideris T, Milto K, Smirnovas V (2015) Polymorphism of amyloid-like fibrils can be defined by the concentration of seeds. PeerJ 3:e1207.
- Sneideris T, Darguzis D, Botyriute A, Grigaliunas M, Winter R, Smirnovas V (2015) pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils. PloS one 10:e0136602.
- Malisauskas R, Botyriute A, Cannon JG, Smirnovas V (2015) Flavone derivatives as inhibitors of insulin amyloid-like fibril formation. PloS one 10:e0121231.
- Milto K, Michailova K, Smirnovas V (2014) Elongation of mouse prion protein amyloid-like fibrils: Effect of temperature and denaturant concentration. PLoS one 9:e94469.
- Milto K, Botyriute A, Smirnovas V (2013) Amyloid-Like Fibril Elongation Follows Michaelis-Menten Kinetics. PLoS one 8:e68684.
Dr. Vytautas Smirnovas
Life Sciences Center
Insitute of Biotechnology
Phone: +370 670 69929
More about the institute faculty: http://bti.vu.lt/en
Department for Research and Innovation
Phone: +370 5 268 7006
More information: https://www.vu.lt/verslui/
Flyer for printing: Group_of_Amyloid_research.pdf