Lu Han



Download Full Text (8.2 MB)


Biopolymers containing chemical groups involved in the formation of adhesive bonds to various substrates (man-made or natural) can be easily found from organisms in nature. The biopolymers utilized by organisms in a process known as quinone tanning contain a unique catecholic amino acid, namely 3,4-dihydroxyphenyl-L-alanine (L-dopa). It has the ability to chelate or couple to the metallic ions or metal oxides that are present at the metal-solution interface. The formation of an insoluble metallo-polymer complex by metal ion bridging at the surface that acts as a stabilizer of the oxide layer can inhibit the process of corrosion. This peculiar capability could be utilized as an environmentally friendly flash rust inhibitor when applied to high strength steels in a humid environment. In the present work, L-dopa containing biopolymers were isolated from the foot of the common blue mussel, Mytilus edulis L. There are five L-dopa containing proteins, named Mytilus edulis Foot Protein 1 through 5 (MeFP 1 through 5) with a wide range of molecular weights from 6-120kDa. The adsorption characteristics of these proteins onto high strength steel (HY80) and 5083 aluminum alloy were observed. The Bradford protein assay was used to detect the solution concentration of non-adsorbed protein onto either alloy. Langmuir isotherm calculations were made to determine the adsorption behavior based on the differences between the original protein concentration in solution at time zero and the protein concentration in solution at each time point. The optimal solution concentration for maximum substrate coverage onto the metal substrate was then determined. Results and data interpretation for the adsorption studies will be presented and discussed.

Publication Date


Project Designation

Graduate Research

Primary Advisor

Douglas C. Hansen

Primary Advisor's Department

Materials Degradation and Electrochemical Engineering (Research Institute-Materials Engineering)


Stander Symposium poster

Adsorption Behavior of Polyphenolic Proteins onto High Strength Steel (HY80) and 5083 Aluminum Alloys