title: Changes in the quaternary structure of amelogenin when adsorbed onto surfaces.
abstract: Amelogenin is a unique protein that self-assembles into spherical aggregates called "nanospheres" and is believed to be involved in controlling the formation of the highly anisotropic and ordered hydroxyapatite crystallites that form enamel. The adsorption behavior of amelogenin onto substrates is of great interest because protein-surface interactions are critical to its function. We report studies of the adsorption of amelogenin onto self-assembled monolayers containing COOH end group functionality as well as single crystal fluoroapatite, a biologically relevant surface. We found that although our solutions contained only nanospheres of narrow size distribution, smaller structures such as dimers or trimers were observed on the hydrophilic surfaces. This suggests that amelogenin can adsorb onto surfaces as small structures that "shed" or disassemble from the nanospheres that are present in solution.
authors.affiliation: Pacific Northwest National Laboratory, Richland, WA 99352, USA. bjtarasevich@pnl.gov
authors.forename: Barbara J
authors.initials: BJ
authors.lastname: Tarasevich
authors.forename: Scott
authors.initials: S
authors.lastname: Lea
authors.forename: William
authors.initials: W
authors.lastname: Bernt
authors.forename: Mark H
authors.initials: MH
authors.lastname: Engelhard
authors.forename: Wendy J
authors.initials: WJ
authors.lastname: Shaw
mesh_terms: D000327:Adsorption; D053523:Amelogenin / Q000737:chemistry*; D003460:Crystallization; D006801:Humans; D018625:Microscopy, Atomic Force; D054118:Nanospheres; D020836:Protein Structure, Quaternary
chemical_list: D053523:Amelogenin