Biomimetic Systems for Hydroxyapatite Mineralization Inspired By Bone and Enamel

Palmer, Liam C.; Newcomb, Christina J.; Kaltz, Stuart R.; Spoerke, Erik David; Stupp, Samuel I.

doi:10.1021/cr8004422

Cited by 966 publications

(897 citation statements)

References 304 publications

(634 reference statements)

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“…Thus, whereas the single-bond binding free energy is slightly greater on the (110) face, the binding energy for the full collagen triple helix is ∼20% larger on the (100) face, suggesting that the stereochemical relationship of collagen to HAP favors better multisite binding on HAP (100) than on HAP (110). [1][2][3][4][5][6][7][8][9][10], and [1][2][3][4][5][6][7][8][9][10][11][12][13] vectors. HAP is a dipolar crystal, constructed of layers of alternating net positive-negative charge that define apparent natural cleavage planes parallel to (100).…”

Section: Results and Analysismentioning

confidence: 99%

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Energetic basis for the molecular-scale organization of bone

Tao

Battle

Pan

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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The remarkable properties of bone derive from a highly organized arrangement of coaligned nanometer-scale apatite platelets within a fibrillar collagen matrix. The origin of this arrangement is poorly understood and the crystal structures of hydroxyapatite (HAP) and the nonmineralized collagen fibrils alone do not provide an explanation. Moreover, little is known about collagen-apatite interaction energies, which should strongly influence both the molecular-scale organization and the resulting mechanical properties of the composite. We investigated collagen-mineral interactions by combining dynamic force spectroscopy (DFS) measurements of binding energies with molecular dynamics (MD) simulations of binding and atomic force microscopy (AFM) observations of collagen adsorption on single crystals of calcium phosphate for four mineral phases of potential importance in bone formation. In all cases, we observe a strong preferential orientation of collagen binding, but comparison between the observed orientations and transmission electron microscopy (TEM) analyses of native tissues shows that only calcium-deficient apatite (CDAP) provides an interface with collagen that is consistent with both. MD simulations predict preferred collagen orientations that agree with observations, and results from both MD and DFS reveal large values for the binding energy due to multiple binding sites. These findings reconcile apparent contradictions inherent in a hydroxyapatite or carbonated apatite (CAP) model of bone mineral and provide an energetic rationale for the molecular-scale organization of bone.biomineralization | bone | protein-mineral interface | dynamic force spectroscopy B one is a natural protein-mineral composite consisting of nonstoichiometric nanometer-scale carbonated apatite crystallites inside a fibrillar protein matrix. The matrix is mainly composed of type I collagen and is organized on multiple length scales (1, 2). At the shortest scale, three polypeptide chains form a triple helix referred to as a tropocollagen molecule that is ∼300 nm in length and 1.5 nm in diameter. These helices are arranged in a quasi-hexagonal bundle in which they overlap and intertwine to form microfibrils containing "hole zones," where there is a gap between the N termini of one helix and the C termini of another (3-5). These microfibrils are further bundled both laterally and longitudinally to form native collagen (3, 4).Within this highly organized scaffold, apatite crystallites form nanometer-scale platelets (6-9) with their [001] axes preferentially aligned parallel to the fibril axis (10-15) and the platelet faces defined by {100} crystal planes (16). Recent in vitro investigations of hydroxyapatite (HAP) formation within collagen fibrils revealed a multistage process in which amorphous calcium phosphate (ACP) first infiltrated through the hole zones and then converted into HAP platelets with initial mineral deposition occurring near the hole zones (11, 13). In vitro transmission electron microscopy (TEM) and atomic force microscop...

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Section: Results and Analysismentioning

confidence: 99%

“…The matrix is mainly composed of type I collagen and is organized on multiple length scales (1,2). At the shortest scale, three polypeptide chains form a triple helix referred to as a tropocollagen molecule that is ∼300 nm in length and 1.5 nm in diameter.…”

mentioning

confidence: 99%

Energetic basis for the molecular-scale organization of bone

Tao

Battle

Pan

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…As shown in Table 3 and discussed above, in the body of mammals, the vast majority of both normal and pathological calcifications consist of non-stoichiometric and ion-doped CaPO 4 , mainly of apatitic structure (Pasteris et al 2008;Palmer et al 2008). At the atomic scale, nano-sized crystals bone apatite exhibit a variety of substitutions and vacancies that make the Ca/P molar ratio distinct from the stoichiometric HA ratio of 1.67.…”

Section: Biological Hard Tissues Of Capomentioning

confidence: 99%

Calcium orthophosphates (CaPO 4 ): Occurrence and properties

Dorozhkin¹

2017

Morphologie

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“…Indeed, functionalizing HA-based materials-as for the case of the bioglass surfaces-to enhance their biocompatibility is a common target [8,9]. Furthermore, understanding the protein/HA contact is of relevance in biomineralization processes [10], since HA grows spontaneously outside the Hench 45S5 Bioglass (45% SiO 2 -24.5% Na 2 O-24.5% CaO-6% P 2 O 5 ), when the latter is contacted with simulated body fluids (SBFs) [11]. In that respect, the HA growth rate is well known to be strongly influenced by the biological composition of the SBF, i.e.…”

Section: Introductionmentioning

confidence: 99%

Ab initio modelling of protein–biomaterial interactions: influence of amino acid polar side chains on adsorption at hydroxyapatite surfaces

Rimola

Corno

Garza

et al. 2012

Phil. Trans. R. Soc. A.

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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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Biomimetic Systems for Hydroxyapatite Mineralization Inspired By Bone and Enamel

Cited by 966 publications

References 304 publications

Energetic basis for the molecular-scale organization of bone

Energetic basis for the molecular-scale organization of bone

Calcium orthophosphates (CaPO 4 ): Occurrence and properties

Ab initio modelling of protein–biomaterial interactions: influence of amino acid polar side chains on adsorption at hydroxyapatite surfaces

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