Interfacial Chemistry and Corrosion of Alloys in Protein-rich Environments

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Our entire biosphere is full of metal-protein interfaces: implant materials in the human body, food in contact with pots, metal surfaces in marine environments, and the production of protein-based drugs are a few examples of these interfaces. Proteins rapidly adsorb on metal surfaces. Under some conditions, this can result in the corrosion (degradation) of the metals. I am an internationally recognized expert in the protein-induced corrosion of metals and have relocated to Canada. I have demonstrated that proteins, organic acids, and amino acids play an important role in the degradation of many metals, including commonly used implant alloys. The degradation requires biomolecule adsorption as well as an exchange of surface-adsorbed and solution biomolecules. The long-term vision for my research program is to advance the understanding of interfacial chemistry and corrosion processes of metals and alloys involving proteins. Over the next 5 years, my research group will determine the role of functional group identity, structure, charge, and hydrophobicity of a given biomolecule (amino acid, peptide, or protein) on corrosion processes. HQP under my supervision will use electrochemical, surface analytical, and solution analytical methods to conduct detailed investigations of the interactions between metals and proteins and their constituent parts. The focus will be on three biomedical alloys, carbon steel (an important construction material), and copper (expected highest interactions with the studied biomolecules). My research group will also investigate the influence of manufacturing processes on the protein-induced corrosion of biomedical alloys. The modern 3D-printing process results in microstructural features, such as melt pool boundaries and porosity, which can initiate corrosion. Traditionally manufactured (cast or wrought) alloys typically have inclusions as corrosion-susceptible weak points. HQP will measure tribocorrosion, the combination of corrosion and wear, and use in-situ atomic force microscopy (AFM) to identify the initiation sites of corrosion. Protein aggregation can result in the misinterpretation of corrosion test results and cause severe health problems. HQP will use dynamic light scattering and in-situ AFM to determine and quantify protein aggregation and precipitation in mixed protein and metal solutions. The effect of the exchange of surface-adsorbed and solution proteins on the amount of metal species in solution and corrosion will be assessed by combined solution analytical and electrochemical techniques with high time resolution. This program will provide hands-on, interdisciplinary training and improve our fundamental understanding of protein-induced corrosion mechanisms of biomedically and industrially relevant metals. HQP will be trained in important soft skills, such as bias awareness, and research areas of great importance for Canada, relevant to construction, pharmaceutical, military, and materials industry.