A Macroscopic Model for the Single-Component Protein Adsorption Isotherm

Electrochemical impedance spectroscopy study of the adsorption behaviour of α-lactalbumin and β-casein at stainless steel

“…The particularly high entropic ðDS 0 ADS Þ value of holo-a-LA suggests that extensive denaturation of a-LA occurs during the adsorption process, relative to both BSA and b-LG. The observed trend in DS 0 ADS values is also consistent with the reported trend in DH D (enthalpy of denaturation evaluated at the melting point temperature) values of 184, 599 and 799 kJ mol À1 for a-LA, b-LG and BSA, respectively [44]. Induced structural changes can lead to a considerable entropy gain, and proteins with low native-state stabilities, such as a-LA and b-LG, possess a strong driving force for adsorption driven by an increase in the conformational entropy of the protein related to the breakdown of native secondary and tertiary structures [45][46][47][48].…”

Protein encapsulation within polyethylene glycol-coated nanospheres. I. Physicochemical characterization

“…The localization of HSA in the particles' structure determines its release characteristics, which may or may not be governed by the physicochemical characteristics of the polymers. Albumin (human or bovine) is well known to give rise to strong hydrophobic interactions and readily adsorbs on various hydrophobic surfaces, 18,19 especially, on PLA. 20 For example, when HSA was used as a surfactant for the preparation of PLA nanospheres, it was reported that a high amount of HSA remained irreversibly adsorbed at their surface and could be visualized by freeze fracture as spherical particles a few nanometers in diameter.…”

“…The amount of HSA on PLA nanospheres at equilibrium was 2.2 mg/m 2 , which is of the same order of magnitude as that observed for other hydrophobic surfaces. 18,19 In contrast, HSA was only slighly adsorbed onto the PEG-PLA nanospheres after a 5-day incubation period (0.15 mg/m 2 ). The low amount of HSA adsorbed onto the PLA-PEG nanospheres shows the effect of the steric protection to ensure resistance against protein adsorption.…”

Electrostatically-controlled protein adsorption onto lipid bilayer: Modeling adsorbate aggregation behavior

“…on geometrical arrangement of protein-lipid contacts. Theoretical description of the proteinmembrane binding is provided by a series of lattice and continuum models of large ligand adsorption to membranes developed by Stankowski [10][11][12], Heimburg & Marsh [13], Chatelier & Minton [14], Talbot [15], Al-Malah [16], Wahlgren et al [17]. In terms of the lattice models lipid bilayer is considered as a regular array of binding contacts (subunits), forming the protein binding sites according to the size and shape of contact region [10][11][12].…”