Amelogenin protein is involved with mineralization of hydroxyapatite (HAP, Ca5(PO4)3OH), the main mineral that comprises tooth enamel. The process of how amelogenin influences mineralization is believed to be related to its affinity for HAP. A quartz crystal microbalance (QCM) sensor has been used to measure amelogenin binding to HAP. QCM studies have been successful because HAP remains adhered to the gold QCM surface in buffer, making binding experiments reproducible. Amorphous calcium phosphate (ACP) is a precursor to HAP and may also bind amelogenin. Studies with ACP have been challenging because ACP does not remain adhered to the gold surface. In this work, a DNA monolayer has been used as a nucleation template with in-line fluidic mixing through a Y-junction to precipitate ACP from calcium chloride and sodium phosphate solutions onto the QCM surface. Pyrophosphate was added to the phosphate solution to maintain calcium phosphate in the amorphous state. This has resulted in a stable growth of ACP on the QCM surface with potential to be used for amelogenin affinity studies. This technique shows significant promise as a reliable method for immobilizing ACP onto a surface and future studies on amelogenin binding to ACP could be performed.

Surface immobilization of amorphous calcium phosphate for protein affinity studies

248th National Meeting (2014)

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