Studies of protein adsorption on polystyrene latex surfaces

摘要: Abstract Adsorption isotherms of bovine serum albumin and y-globulin on polystyrene latices are reported. Under certain conditions, for each protein, the exhibit bimodal adsorption characteristics in confirmation earlier reports. The maximal adsorbance values near expectation a close-packed monolayer. It is noted that ratio lower to upper plateau 0.40 γ-globulin case 0.56 examples. hydrodynamic thickness adsorbed layer as function amount protein has been characterized by photon correlation spectroscopy analysis. No evidence multilayer at higher coverages or conformational “flattening” regime could be established. Based this information, we propose mechanism which does not require major changes, postulates existence critical supersaturation homogeneous nucleation two-dimensional surface “crystal” protein. Below concentration, development ordered structure kinetically limited finite configurational relaxation time surface. In regime, less dense partially organized “glassy” monolayer found. involves random independent isolated molecules.