Neutron reflectometry studies of the adsorbed structure of the amelogenin, LRAP.

ABSTRACT: Amelogenins make up over 90% of the protein present during enamel formation and have been demonstrated to be critical in proper enamel development, but the mechanism governing this control is not well understood. Leucine-rich amelogenin peptide (LRAP) is a 59-residue splice variant of amelogenin and contains the charged regions from the full protein thought to control crystal regulation. In this work, we utilized neutron reflectivity (NR) to investigate the structure and orientation of LRAP adsorbed from solutions onto molecularly smooth COOH-terminated self-assembled monolayer (SAM) surfaces. Sedimentation velocity (SV) experiments revealed that LRAP is primarily a monomer in saturated calcium phosphate (SCP) solutions (0.15 M NaCl) at pH 7.4. LRAP adsorbed as ∼32 Å thick layers at ∼70% c

SUBMITTER: Tarasevich BJ 

PROVIDER: S-EPMC3634335 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature