Adsorption of myoglobin onto various synthetic hydroxyapatite particles

Kandori, Kazuhiko; Fudo, Aya; Ishikawa, Tatsuo

doi:10.1039/a909396f

Cited by 61 publications

(60 citation statements)

References 18 publications

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“…As for point (i), adsorption isothermal experiments as well as conventional high-resolution spectroscopy studies have been performed to determine both macroscopic quantities and the actual interaction interface of statherin [14][15][16][17][18][19][20], myoglobin [21,22], amelogenin [23,24], bovine serum albumin [24][25][26], bovine serum fibrinogen [26], lysozome [25,26] and proline-rich protein PRP1 [27] upon HA adsorption. Most of these papers conclude that proteins are generally adsorbed by electrostatic forces of different strength depending on the protein structure and AA sequence.…”

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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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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“…Thus a change in the net charge of the substrate induced by the adsorption of the polyampholyte has only a small influence on the electrostatic interaction with the protein. Therefore, it is not reasonable to argue that the electrostatic interaction explains the adsorption behaviour of myoglobin [44], Also the increased attraction between phosphate ions and subtrate induced by preadsorbed polyampholyte would decrease the myoglobin adsorption. The increase in adsorption of myoglobin is not explained by electrostatic interactions or changes in the hydrophilic properties of the substrate.…”

Section: Resultsmentioning

confidence: 99%

Protein adsorption on preadsorbed polyampholytic monolayers

Mahltig

Werner

Müller

et al. 2001

Journal of Biomaterials Science, Polymer Edition

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The adsorption behaviour of five different globular proteins on pure silicon substrates and on preadsorbed polyampholytic monolayers has been investigated as a function of protein concentration.. The prelayers were prepared by adsorption of the ampholytic diblock copolymer poly(methacrylic acid)-block-poly((dimethylamino)ethyl methactylate) (PMAA-b-PDMAEMA). This polyampholyte adsorbs in densely packed micelles directly from aqueous solution. Ellipsome-try was used to determine the amount of adsorbed polyampholyte and protein While ATR-IR spectroscopy gives information about the adsorption and desorption behaviour of the preadsorbed polyam-pholytic layer, the lateral structures of the dried films were investigated by scanning force microscopy (SFM). The amount of protein adsorbed was found to be strongly influenced by the preadsorbed polyampholyte compared to the adsorption on the pure silicon substrates. No displacement of the poly ampholyte by the proteins was detected. In most cases the protein adsorption was reduced by the preadsorbed polyampholytic layer. The observed trends are explained by the change in electrostatic and hydrophilic characteristics of the substrates. Furthermore, the entropy of adsorption has to be taken into account

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“…However, it has been reported that MGB can adsorb onto HAp. 26) Actually, MGB adsorption onto nano-HAp (e.g. CP-4) has also been described in this paper.…”

Section: Adsorption Of Proteins Onto Nano-hapsmentioning

confidence: 99%

“…26), 27) Five mg of nano-HAp particles was mixed in 1 mL of a 0.5 mg/mL protein solution dissolved in 11 mM of a phosphate buffer solution (pH 7.4). The mixture was stirred overnight at 4°C.…”

Section: Protein Adsorption On Nano-hapmentioning

confidence: 99%

Hydrothermal synthesis of hydroxyapatite nanoparticles and their protein adsorption behavior

Nagata

Yamauchi

Tomita

et al. 2013

J. Ceram. Soc. Japan

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Protein adsorption on hydroxyapatite particles with different morphologies was investigated. The nano-sized hydroxyapatite (nano-HAp) was prepared using calcium nitrate tetrahydrate [Ca(NO 3 ) 4 ·4H 2 O] and diammonium hydrogen phosphate [(NH 4 ) 2 -HPO 4 ] by using a hydrothermal method with varying synthesis temperature and pH conditions. The adsorption properties of proteins onto nano-HAp were studied using three types of proteins: bovine serum albumin (BSA, an acidic protein), myoglobin (MGB, a neutral protein), and lysozyme (LSZ, a basic protein). The adsorption amount of BSA and LSZ per unit specific surface area of nano-HAp increased as the crystallinity improved. In contrast, the improvement in the crystallinity of HAp decreased adsorption affinity to MGB. This adsorption behavior on nano-HAp would be considered by the specific binding of the C-or Psite on HAp towards acidic or basic proteins, respectively.

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Adsorption of myoglobin onto various synthetic hydroxyapatite particles

Cited by 61 publications

References 18 publications

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

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

Protein adsorption on preadsorbed polyampholytic monolayers

Hydrothermal synthesis of hydroxyapatite nanoparticles and their protein adsorption behavior

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