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Interaction of bovine serum albumin and lysozyme with stainless steel studied by time of flight secondary ion mass spectrometry and x-ray photoelectron spectroscopy.


Langmuir. 2012 Nov 1;


Authors: Hedberg YS, Killian MS, Blomberg E, Virtanen S, Schmuki P, Odnevall Wallinder I


Abstract

An in-depth mechanistic understanding of the interaction between stainless steel surfaces and proteins is essential from a corrosion and protein-induced metal release perspective when used as surgical implants and in food applications. The interaction between lysozyme (LSZ) from chicken egg white and bovine serum albumin (BSA) and AISI 316L stainless steel surfaces was studied ex-situ by means of X-ray photoelectron spectroscopy (XPS) and time-of-flight secondary ion mass spectrometry (ToF-SIMS) after different adsorption time periods (0.5, 24, and 168 h). The effect of XPS measurements, storage (ageing), sodium dodecyl sulfate (SDS), elevated temperature (up to 200°C) on the protein coatings as well as changes in surface oxide composition were in addition investigated. Both BSA and LSZ adsorption induced an enrichment of chromium in the oxide layer. BSA induced significant changes to the entire oxide while LSZ only induced a depletion of iron at the utmost layer. SDS was not able to remove pre-adsorbed proteins completely from aged samples, despite its high concentration and relatively long treatment time (up to 36.5 h), but induced partial denaturation of the protein coatings. High temperature treatment (200°C) and XPS exposure (X-ray irradiation and/or photoelectron emission) induced significant denaturation of both proteins. The heating treatment up to 200°C removed some proteins, far from all. Amino acid fragment intensities determined from ToF-SIMS are discussed in terms of significant differences with adsorption time, between the proteins, and between freshly adsorbed and aged samples. Stainless steel - protein interactions were shown to be strong and protein-dependent. The findings assist in the understanding of previous studies of metal release and surface changes upon exposure to similar protein solutions.

PMID: 23116183 [PubMed - as supplied by publisher]