Differential Expression of Hard Tissue Proteins in Hypomineralized Second Primary Molars in Comparison to Normal Teeth.

Objective: This study aims to identify the proteins in hypomineralized second primary molars (HSPMs) and correlate their function in Amelogenesis. HSPM is a qualitative defect of the enamel of the second primary molars with no clear etiology.

Material And Methods: Total protein quantification was performed using the Bradford Protein Assay, followed by the electrophoretic separation of samples using 2D-Gel electrophoresis to identify the proteins.

The use of N-terminal immobilization of PTH(1-34) on PLGA to enhance bioactivity.

The objective of this work was to control the orientation of bioactive molecules immobilized on a biodegradable substrate to improve their accessibility for binding to cell surface receptors and, therefore, to increase bioactivity. The osteotropic peptide, parathyroid hormone (1-34) (PTH(1-34)), was used to demonstrate the approach. To this end, the intrinsic N-terminal serine residue was oxidized to create an aldehyde group that specifically bound to hydrazide-derivatized poly(lactide-co-glycolide) under neutral conditions to form a hydrazone bond.