| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5366395 | Applied Surface Science | 2012 | 6 Pages |
The adsorption of lysine (Lys) on hydroxyapatite (HA) (1Â 0Â 0) surface was studied using density functional theory calculations within the generalized gradient approximation framework. The optimal adsorption pattern was identified from a number of interactive Lys-HA structures. The carbonyl-O, amine-H and CÉ-H atoms are active sites in Lys that interact directly with the Ca ion and phosphate-O atoms on the HA (1Â 0Â 0) surface, respectively. Multiple interactions were noted between Lys and HA surface. The adsorption is mainly stabilized by the CaO ionic bonding, followed by hydrogen bond and/or van der Waals interaction between phosphate-O and Lys-HA. Both the Lys and HA surface structures are subjected to some changes upon adsorption. The zwitterionic form of Lys was found more stable on the HA (1Â 0Â 0) surface than its neutral form. Our calculations reveal the structural characteristics and their variations for the Lys-HA systems, which are essential for understanding the interaction mechanism of biomolecules with inorganic biomaterials.
Graphical abstractDownload full-size imageHighlights⺠Conformers of Lys on HA (1 0 0) surface are identified. ⺠Multiple interactions that favor the Lys adsorption are revealed. ⺠Strong ionic bonding is formed between carbonyl-O in Lys and Ca ion on HA surface. ⺠Both Lys and HA structures are subjected to changes upon adsorption.
