| Ab initio modelling of protein-biomaterial interactions: influence of amino acid polar side chains on adsorption at hydroxyapatite surfaces. | |
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MedLine Citation:
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PMID: 22349252 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The adsorption from the gas phase of five different amino acids (AAs), namely Gly, Ser, Lys, Gln and Glu, on three surface models of hexagonal hydroxyapatite (HA) has been studied at B3LYP level with Gaussian type basis set within a periodic approach. The AA adsorption was simulated on the (001) and (010) stoichiometric surfaces, the latter both in its pristine and water-reacted form. Low/high AA coverage has been studied by doubling the HA unit cell size. The AAs have been docked to the HA surfaces following the electrostatic complementarity between the electrostatic potentials of AA and the bare HA. Gly adsorbs as a zwitterion at the (001) surface, whereas at the (010) ones, the proton of the COOH group is transferred to the surface resulting in an HA(+)/Gly(-) ion pair. For the other AAs, the common COOH-CH-NH(2) moiety behaves like in Gly, while the specific side-chain functionalities adsorb at the HA surfaces by maximizing electrostatic and H-bond interactions. The interactions between the side chains and the HA surface impart a higher stability compared with the Gly case, with Glu being the strongest adsorbate owing to its high Ca affinity and H-bond donor propensity. For AAs of large size, the adsorption is more favourable in conditions of low coverage as repulsion between adjacent AAs is avoided. For all considered AAs, the strongest interaction is always established on the (010) faces rather than on the (001) one, therefore suggesting an easier growth along the c-direction of HA crystals from AA solutions. |
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Authors:
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Albert Rimola; Marta Corno; Jorge Garza; Piero Ugliengo |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Philosophical transactions. Series A, Mathematical, physical, and engineering sciences Volume: 370 ISSN: 1364-503X ISO Abbreviation: Philos Trans A Math Phys Eng Sci Publication Date: 2012 Mar |
Date Detail:
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Created Date: 2012-02-21 Completed Date: 2012-05-01 Revised Date: 2013-04-24 |
Medline Journal Info:
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Nlm Unique ID: 101133385 Medline TA: Philos Trans A Math Phys Eng Sci Country: England |
Other Details:
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Languages: eng Pagination: 1478-98 Citation Subset: IM |
Affiliation:
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Departament de Química, Universitat Autònoma de Barcelona, Bellaterra 08193, Spain. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Adsorption Binding Sites Coated Materials, Biocompatible / chemistry* Computer Simulation Durapatite / chemistry* Models, Chemical* Models, Molecular* Protein Binding Proteins / chemistry*, ultrastructure* |
| Chemical | |
Reg. No./Substance:
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0/Coated Materials, Biocompatible; 0/Proteins; 1306-06-5/Durapatite |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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