The adhesive polyphenolic protein from marine mussels is a dopa- containing protein with a significant potential for metal complexation at pH 6-10. This holds promise for the development of new bioadhesives, because current adhesives are subverted by the presence of water on surfaces. In complexing or chelating metals on dental or orthopaedic implants, for example, dopa- containing proteins could transcend the weak boundary layer formed by water on the metal surface and displace oxides always present on metal surfaces in a moist environment. This proposal attempts to 1) demonstrate that specific adsorption of dopa-containing proteins and peptides can be quantitatively interpreted in terms of surface coordination processes; 2) illustrate with experimentally determined surface complexation equilibrium constants, the extent of adsorption of dopa-peptides can be predicted as a function of pH; 3) to determine whether the tendency of forming surface oxide complexes is similar to that for forming complexes with metal ions in solution. The methodology for these studies will be by potentiometric and spectroscopic monitoring of metal-ligand titrations.
| Rzepecki, L M; Waite, J H (1991) alpha,beta-Dehydro-3,4-dihydroxyphenylalanine derivatives: rate and mechanism of formation. Arch Biochem Biophys 285:27-36 |
| Rzepecki, L M; Nagafuchi, T; Waite, J H (1991) alpha,beta-Dehydro-3,4-dihydroxyphenylalanine derivatives: potential schlerotization intermediates in natural composite materials. Arch Biochem Biophys 285:17-26 |
| Taylor, S W; Molinski, T F; Rzepecki, L M et al. (1991) Oxidation of peptidyl 3,4-dihydroxyphenylalanine analogues: implications for the biosynthesis of tunichromes and related oligopeptides. J Nat Prod 54:918-22 |
| Rzepecki, L M; Waite, J H (1989) A chromogenic assay for catecholoxidases based on the addition of L-proline to quinones. Anal Biochem 179:375-81 |
