Hydroxyapatite formation on graphene oxide modified with amino acids: arginine versus glutamic acid.

Abstract

Hydroxyapatite (HA, Ca5(PO4)3OH) is the main inorganic component of hard tissues, such as bone and dentine. HA nucleation involves a set of negatively charged phosphorylated proteins known as non-collagenous proteins (NCPs). These proteins attract Ca(2+) and PO4(3-) ions and increase the local supersaturation to a level required for HA precipitation. Polar and charged amino acids (AAs) are highly expressed in NCPs, and seem to be responsible for the mineralizing effect of NCPs; however, the individual effect of these AAs on HA mineralization is still unclear. In this work, we investigate the effect of a negatively charged (Glu) and positively charged (Arg) AA bound to carboxylated graphene oxide (CGO) on HA mineralization in simulated body fluids (SBF). Our results show that Arg induces HA precipitation faster and in larger amounts than Glu. We attribute this to the higher stability of the complexes formed between Arg and Ca(2+) and PO4(3-) ions, and also to the fact that Arg exposes both carboxyl and amino groups on the surface. These can electrostatically attract both Ca(2+) and PO4(3-) ions, thus increasing local supersaturation more than Glu, which exposes carboxyl groups only.