Conformational changes of globular proteins upon adsorption on a hydrophobic surface

Abstract

This paper presents a study of protein adsorption and denaturation using coarse-grained Monte Carlo simulations with simulated annealing. Intermolecular interactions are modeled using the Miyazawa-Jernigan (MJ) knowledge-based potential for an implicit solvent. Three different hydrophobicity scales are tested for adsorption of fibronectin on a hydrophobic surface. The hydrophobic scale BULDG was chosen for further analysis due to its greater stability during heating and its partial regenerative ability upon slow cooling. Differences between helical and sheet structures are observed upon denaturation -α-helices undergo spreading of their native helical order to an elliptical perturbed shape, while β-sheets transform into random coils and other more structured conformations. Electronic calculations carried out on rebuilt all-atom coordinates of adsorbed lysozymes revealed consistent destabilization of helices, while beta sheets show a greater variety of trends.

Aminolysis as a surface functionalization method of aliphatic polyester nonwovens: impact on material properties and biological response

“…It is reported that protein adsorption on hydrophobic surfaces can lead to their denaturation, which can make them unable to bind cells. 37 It was experimentally found that too high hydrophilicity could also be unfavourable for cell attachment. 38 Hence, it appears that moderate wettability provides the proper amount of adsorbed proteins as well as unchanged conformation, which results in good cell response.…”

Synthesis and Characterization of Cholesteryl Conjugated Lysozyme (CHLysozyme)

“…Chemical modification of hydrophobic groups to proteins have not been reported to the same degree. In native proteins, the hydrophobic residues are internally situated [22,23], although these residues can be exposed to the surface if the protein is denatured by chemical or physical stress [24,25]; moreover, protein aggregation has been assumed to be due to hydrophobic interaction between denatured proteins with surface-exposed hydrophobic residues [26,27]. Furthermore, aggregation affects biological activity and causes immunogenicity, and thus must be controlled during development of biopharmaceuticals [28,29].…”

Surface Activity as a Crucial Factor of the Biological Actions of Ole e 1, the Main Aeroallergen of Olive Tree (Olea europaea) Pollen

“…This observation suggests that lipid domains can act as nucleation sites for the allergen, in which new noncovalent interactions could be established between neighboring molecules, due to the interfacial exposition of hydrophobic residues that are normally hidden in the protein structure. 29 The coexistence of protein and DPPC at the interface suggests the existence of several mechanisms that could take place in vivo during the first stages of allergen sensitization. On one hand, Ole e 1 adsorption could impair or abolish normal surface activity of pulmonary surfactant, which is crucial particularly during expiration.…”