Secondary Structure of Proteins Adsorbed onto or Embedded in Polyelectrolyte Multilayers

Abstract

The structural changes of bovine serum albumin (BSA) and hen egg white lysozyme (HEL) upon their adsorption onto the surface or their embedding into the interior of poly(allylamine hydrochloride)-(poly(styrenesulfonate) (PAH-PSS) multilayer architectures were investigated by attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy. The presence of the polyelectrolytes seems, as previously observed for fibrinogen (J. Phys. Chem. B 2001, 105, 11906-11916), to prevent intermolecular interactions and, thus, protein aggregation at ambient temperature. The secondary structure of the proteins was somewhat altered upon adsorption onto the polyelectrolyte multilayers. The structural changes were larger when the charges of the multilayer outer layer and the protein were opposing. The adsorption of further polyelectrolyte layers onto protein-terminated architectures (i.e., embedding the proteins into a polyelectrolyte multilayer) did not cause considerable further changes in their secondary structures. The capacity of the polyelectrolyte architectures to delay the formation of intermolecular beta-sheets upon increasing temperatures was not uniform for the studied proteins. PSS in contact with HEL could largely prevent the heat-induced aggregation of HEL. In contrast, PAH had hardly any effect on the aggregation of BSA. The differences are explained on the basis of protein-polyelectrolyte interactions, affected mostly by the nature and the strength of the ionic interactions between the polyelectrolyte-protein contact surfaces.

Polyelectrolyte Multilayers on Silica Surfaces: Effect of Ionic Strength and Sodium Salt Type

“…proteins) could be adsorbed. In the literature, [14][15][16] several studies of protein adsorption on previously formed polyelectrolyte multilayers could be found. Müller and coworkers [14] examined the sorption of HSA on poly(ethyleneimine)/poly(acrylic acid) multilayers using ATR FTIR spectroscopy, while Gergelly et al [15] analysed adsorption of the same protein on poly(L-lysine)/ poly(glutamic acid) multilayer by Optical Waveguide LightMode Spectroscopy (OWLS) and AFM.…”

“…The secondary structure of lysozyme and bovine serum albumin (BSA) adsorbed onto PAH/PSS multilayers was investigated by Schaaf and co-workers. [16] They showed that the secondary structure of the proteins was somewhat altered upon adsorption onto the polyelectrolyte multilayers and that P the structural changes were larger when the charges of the multilayer outermost layer and the protein were opposing. A special and very promising case is the possible application of polyelectrolyte multilayers as antibacterial coatings.…”

Casein Aggregates Built Step-by-Step on Charged Polyelectrolyte Film Surfaces Are Calcium Phosphate-cemented

“…We have shown earlier that proteins and proteolipid membranes can adsorb onto such polyelectrolyte films, and their native secondary structure is little affected (11). In addition, once a protein has been adsorbed, its secondary structure is stabilized/fixed by the interaction with the polyelectrolyte film (12,13).…”

Electrokinetic Study of Bovine Serum Albumin Adsorption on Previously Formed PAH/PSS Multilayer

“…proteins) could be adsorbed. In the literature, [2][3][4] various examples of investigation of the adsorption of different proteins on previously formed multilayers could be found. Müller and coworkers 2 examined the adsorption of human serum albumin (HSA) on poly(ethyleneimine)/poly(acrylic acid) multilayers using ATR FTIR spectroscopy, while Gergelly et al 3 analysed the adsorption of the same protein on poly(L-lysine)/poly(glutamic acid) multilayer by Optical Waveguide Light-Mode Spectroscopy (OWLS) and AFM.…”

“…Müller and coworkers 2 examined the adsorption of human serum albumin (HSA) on poly(ethyleneimine)/poly(acrylic acid) multilayers using ATR FTIR spectroscopy, while Gergelly et al 3 analysed the adsorption of the same protein on poly(L-lysine)/poly(glutamic acid) multilayer by Optical Waveguide Light-Mode Spectroscopy (OWLS) and AFM. The secondary structure of bovine serum albumin (BSA) adsorbed onto PAH/PSS multilayers was also investigated by Schaaf and coworkers 4 and it was observed that PAH as terminal layer has practically no effect on aggregation of BSA. In our earlier paper 5 we investigated the adsorption of BSA on previously formed poly(allylamine hydrochloride)/poly(sodium 4-styrenesulphonate) (PAH/PSS) multilayer with PAH being a terminal layer by stagnation point optical reflectometry.…”