Salt induced reduction of lysozyme adsorption at charged interfaces. (20th May 2015)

• Record Type: Journal Article
• Authors: Göhring, Holger; Paulus, Michael; Salmen, Paul; Wirkert, Florian; Kruse, Theresa; Degen, Patrick; Stuhr, Susan; Rehage, Heinz; Tolan, Metin
• Is Part Of: Journal of physics. Volume 27:Number 23(2015)
• Publication Date: 2015-05-20
• Subjects: protein adsorption -- charged interfaces -- x-ray reflectivity; Condensed matter -- Periodicals; Matière condensée -- Périodiques; Vaste stoffen; Vloeistoffen; Natuurkunde; Electronic journals; Computer network resources; 530.4105
• DOI: 10.1088/0953-8984/27/23/235103
• Languages: English
• ISSNs: 0953-8984

Abstract

Abstract: A study of lysozyme adsorption below a behenic acid membrane and at the solid–liquid interface between aqueous lysozyme solution and a silicon wafer in the presence of sodium chloride is presented. The salt concentration was varied between 1 mmol L −1 and 1000 mmol L −1 . X-ray reflectivity data show a clear dependence of the protein adsorption on the salt concentration. Increasing salt concentrations result in a decreased protein adsorption at the interface until a complete suppression at high concentrations is reached. This effect can be attributed to a reduced attractive electrostatic interaction between the positively charged proteins and negatively charged surfaces by charge screening. The measurements at the solid–liquid interfaces show a transition from unoriented order of lysozyme in the adsorbed film to an oriented order with the short protein axis perpendicular to the solid–liquid interface with rising salt concentration.