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Computer simulations of the interaction of bio-molecules with hydroxyapatite surfaces in aqueous environment
| Content Provider | Semantic Scholar |
|---|---|
| Author | Almora-Barrios, Neyvis Leeuw, N. H. De |
| Copyright Year | 2009 |
| Abstract | In view of the importance of the hydroxyapatite/ collagen composite of both natural bone tissue and in synthetic biomaterials, we have employed a combination of electronic structure calculations based on the Density Functional Theory and Molecular Dynamics simulations to investigate the interaction with two major hydroxyapatite surfaces of the three amino acids that largely make up the collagen matrix, as well as a peptide strand of the same residues (glycine, proline and hydroxyproline). We have performed full geometry optimisations of the hydroxyapatite surfaces with adsorbed amino acid molecules to obtain the optimum substrate/adsorbate structures and interaction energies, both in vacuo and in a liquid water environment. An aqueous environment is added through the explicit introduction of water molecules in the simulation of the dynamic behaviour. The calculations show that the amino acids, as well as the complete peptide are capable of forming multiple interactions with surface species, particularly if they can bridge between two surface calcium ions. The binding energies range from 291 kJ mol for glycine on the (0001) surface to 610 kJ mol for hydroxy-proline on the ) 0 1 01 ( surface. The large adsorption energies are due to a wide range of interactions between adsorbate and surface, including proton transfer from the adsorbates to surface OH or PO4 groups. Similar to the amino acides, the Gly-Pro-Hyp peptide also binds more strongly to the hydroxyapatite ) 0 1 01 ( surface; indeed, in an aqueous environment only binding at this surface is thermodynamically favourable, which suggest that, in the presence of the collagen matrix, the hydroxyapatite crystal would grow more rapidly in the (0001) direction than in the ) 0 1 01 ( direction, in agreement with the naturally observed bone morphology. A thrust for early skeletal evolution provided by ocean chemistry G. ALOISI Institute for Marine Sciences (IFM-GEOMAR), Wischhofstrasse 1-3, 24148 Kiel, Germany. UMR 5125 PEPS, CNRS; Université Lyon 1, Campus de le DOUA, 69622 Villeurbanne Cedex, France. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://goldschmidtabstracts.info/2009/31.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
