Effect of substituents in chlorin e derivatives on the loading efficiency of the photosensitizer into the liposome membrane and their biological activity.

In this work, we incorporated the hydrophobic alkylamide and hydroxyalkylamide derivatives of chlorin e into the lipid bilayer of liposomes. We obtained the data on the effectiveness of incorporation of studied compounds and have determined the size of liposomes and their stability when stored in liquid form. We also investigated the bioactivity of chlorin photosensitizers and compared the photodynamic activity of studied compounds in free and liposomal forms.

Salt- and pH-induced desorption: Comparison between non-aggregated and aggregated mussel adhesive protein, Mefp-1, and a synthetic cationic polyelectrolyte.

Mussel adhesive proteins are of great interest in many applications due to their ability to bind strongly to many types of surfaces under water. Effective use such proteins, for instance the Mytilus edulis foot protein - Mefp-1, for surface modification requires achievement of a large adsorbed amount and formation of a layer that is resistant towards desorption under changing conditions. In this work we compare the adsorbed amount and layer properties obtained by using a sample containing small Mefp-1 aggregates with that obtained by using a non-aggregated sample.

Nanostructured composite layers of mussel adhesive protein and ceria nanoparticles.

Mussel adhesive proteins are known for their high affinity to a range of different surfaces, and they therefore appear as ideal candidates for producing thin inorganic-organic composite films with high robustness. In this work we explore the possibility of making cohesive films utilizing layer-by-layer deposition of the highly positively charged mussel adhesive protein, Mefp-1, and negatively charged ceria nanoparticles. This particular material combination was chosen due to recent findings that such films provide good corrosion protection.

Kinetic and equilibrium aspects of adsorption and desorption of class II hydrophobins HFBI and HFBII at silicon oxynitride/water and air/water interfaces.

Hydrophobins are relatively small globular proteins produced by filamentous fungi. They display unusual high surface activity and are implied as mediators of attachment to surfaces, which has resulted in high scientific and technological interest. In this work we focus on kinetic and equilibrium aspects of adsorption and desorption properties of two representatives of class II hydrophobins, namely HFBI and HFBII, at a negatively charged hydrophilic solid/water interface and at the air/water interface.

Adsorption of Mefp-1: influence of pH on adsorption kinetics and adsorbed amount.

Mussel adhesive proteins have received considerable attention due to their ability to bind strongly to many surfaces under water. Key structural features of these proteins include a large number of 3,4-dihydroxyphenyl-L-ALANIN (DOPA) and positively charged lysine residues. We elucidate the effects of solution pH, in the pH range 3-9, on adsorption kinetics, adsorbed amount, and layer structure on silicon oxynitride by employing Dual Polarization Interferometry.