Selected papers

Characterization of AMBN I and II Isoforms and Study of Their Ca<sup>2+</sup>-Binding Properties
Characterization of AMBN I and II Isoforms and Study of Their Ca2+-Binding Properties
International Journal of Molecular Sciences 21 (23): 9293 (2020)
Ameloblastin (Ambn) as an intrinsically disordered protein (IDP) stands for an important role in the formation of enamel—the hardest biomineralized tissue commonly formed in vertebrates. The human ameloblastin (AMBN) is expressed in two isoforms: full-length isoform I (AMBN ISO I) and isoform II (AMBN ISO II), which is about 15 amino acid residues shorter than AMBN ISO I. The significant feature of AMBN—its oligomerization ability—is enabled due to a specific sequence encoded by exon 5 present at the N-terminal part in both known isoforms. In this study, we characterized AMBN ISO I and AMBN ISO II by biochemical and biophysical methods to determine their common features and differences. We confirmed that both AMBN ISO I and AMBN ISO II form oligomers in in vitro conditions. Due to an important role of AMBN in biomineralization, we further addressed the calcium (Ca2+)-binding properties of AMBN ISO I and ISO II. The binding properties of AMBN to Ca2+ may explain the role of AMBN in…
Intrinsically disordered protein domain of human ameloblastin in synthetic fusion with calmodulin increases calmodulin stability and modulates its function
International Journal of Biological Macromolecules 168: 1-12 (2021)

Latest publications

Production of recombinant human ameloblastin by a fully native purification pathway
Protein Expression and Purification 198: 106133 (2022)
TRPM5 Channel Binds Calcium-Binding Proteins Calmodulin and S100A1
Biochemistry 61 (6): 413–423 (2022)
TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
Heliyon 7 (12): e08490 (2021)
The order of PDZ3 and TrpCage in fusion chimeras determines their properties—a biophysical characterization
Protein Science 30 (8): 1653-1666 (2021)