Albumin binding and insertion into PS-b-PEO monolayers at air-water interface

Interaction of human serum albumin with poly(styrene)-b-poly(ethylene oxide) (PS-b-PEO) monolayer at air/solution interface was studied by measuring surface pressure. The density of PEO chains in the monolayer was controlled using Langmuir trough barriers. The thickness of PS-b-PEO monolayer prior to and after albumin adsorption was computed from in situ surface plasmon resonance (SPR) measurements. Depending on the initial PEO surface density the surface pressure kinetics of albumin insertion displayed two different regimes: below the PEO "pancake-brush" transition albumin binding was initially very rapid and itself induced the "pancake-brush" transition in the monolayer, and above the "pancake-brush" transition where some albumin penetration into the free PS-b-PEO monolayer still occurred into the PEO "brush". In the case of SPR-immobilized monolayer, more than 0.1 PEO chain/nm(2) was required to inhibit albumin or ferritin adsorption. A half-reduction of albumin adsorption required approx. three-fold higher PEO surface density than the half-reduction of ferritin adsorption.