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Flash rusting is a corrosion process in which steel rapidly oxidizes upon contact with air at a high relative humidity. The ultimate goal of this research is to develop a water-soluble and environmentally friendly corrosion inhibitor that will inhibit flash rust on high strength steel (HY80). Several proteins involved in the formation of the adhesive byssal threads by the blue mussel Mytilus edulis L have been identified for their potential as corrosion inhibitors. The most important feature of these biomolecules for corrosion prevention applications is the presence of a post-translationally modified amino acid L-3, 4 dihydroxyphenylalanine (L-dopa). L-dopa has a well characterized ability to form strong bonds with metal ions, thus stabilizing the metal surface and inhibiting corrosion. In addition, enzymatically treated L-dopa containing proteins can participate in crosslinking reactions, which have been shown to lead to a thicker and more durable protein layer. In this study, HY80 steel coupons were treated with varying amounts of MAP-1, the largest and most well-characterized of the five mussel proteins, in 0.05M phosphate buffer at pH 7.0 and exposed in an accelerated atmospheric corrosion chamber maintained at 40°C and 100% relative humidity. For comparison, identical HY80 samples were treated with a commercially available flash rust corrosion inhibitor under identical exposure conditions. The results indicate that the corrosion inhibiting behavior of the cross-linked protein may be contingent on the presence of an air-formed oxide layer. Current results suggest that the mussel protein is nearly as effective as the commercial inhibitor at a similar concentration, which shows that the protein could potentially serve as an environmentally friendly replacement for current flash rust inhibitors.

Publication Date


Project Designation

Graduate Research

Primary Advisor

Douglas C. Hansen

Primary Advisor's Department

Chemical and Materials Engineering


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