The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces.

ABSTRACT: Amelogenin 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 proteins onto substrates is very important because protein-surface interactions are critical to its function. We have previously used LRAP, a splice variant of amelogenin, as a model protein for the full-length amelogenin in solid-state NMR and neutron reflectivity studies at interfaces. In this work, we examined the adsorption behavior of LRAP in greater detail using model self-assembled monolayers containing COOH, CH(3), and NH(2) end groups as substrates. Dynamic light scattering (DLS) experiments indicated that LRAP in phosphate buffered saline and solutions containing low concentrations of calcium a

SUBMITTER: Tarasevich BJ 

PROVIDER: S-EPMC3084684 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature