Molecular Modeling and Characterization of a Mussel Adhesive Protein (Mefp-5)
The blue mussel, Mytilus edulis, secretes adhesive proteins to facilitate adhesion to a variety of substrates. Several Mytilus edulis foot proteins (MeFP) have been isolated and characterized. MeFP-5 is said to be the most adhesive of these proteins, and has a comparatively large molecular percentage of L-Dopa when examined against MeFP proteins 1-4 at over 25% L-Dopa, if full conversion from tyrosine occurs. The catechol functional group of L-Dopa complexes with Fe3+ to form organometallic linkages, but how L-Dopa in MeFP-5 is interacting with an iron oxide surface, and if the lysine amino acids adjacent to L-Dopa help to facilitate formation of the epoxy-like barrier on iron oxides, is unknown. This project focuses on evaluating the orientation of the catechol groups in L-Dopa through molecular modeling, generating a 3D model of an iron oxide surface, characterizing regions of MeFP-5 which are most likely to complex with Fe3+, and altering the amino acid composition of MeFP-5 to attempt to maximize adhesive properties and explore possibilities for creating a synthetic analog. Modeling is done in the programs ChemDraw® and Chem3D® (PerkinElmer) to analyze protein structure and the catechol positioning of L-Dopa within the protein MeFP-5. To validate and refine the model, experimental data of MeFP-5 adsorbed onto HY80 steel using Raman infrared spectroscopy have been used to determine what interaction the lysine and L-Dopa functional groups in MeFP-5 have on the steel surface. These data have been incorporated into the 3-dimensional model of the protein-metal interface.
Douglas C Hansen, Karolyn M Hansen
Primary Advisor's Department
Stander Symposium poster
"Molecular Modeling and Characterization of a Mussel Adhesive Protein (Mefp-5)" (2018). Stander Symposium Posters. 1432.