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Secondary structure analysis of proteins embedded in spherical polyelectrolyte brushes by FT-IR spectroscopy

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2004

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Ballauff, Matthias

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Analytical Chemistry. 2004, 76(10), pp. 2813-2819. ISSN 0003-2700. Available under: doi: 10.1021/ac0354692

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The adsorption of bovine serum albumin (BSA), bovine β-lactoglobulin, and bovine pancreatic ribonuclease A onto spherical polyelectrolyte brushes (SPB) is reported. The SPB consist of narrowly distributed poly(styrene) core particles (diameter 100 nm) onto which linear chains of anionic polyelectrolytes are grafted. The polyelectrolyte shell consists of either the weak polyelectrolyte poly(acrylic acid) or the strong polyacid poly(styrenesulfonate). The SPB particles are dispersed in H2O at room temperature. The secondary structure of the proteins was investigated by Fourier transform infrared spectroscopy in transmission mode before and during adsorption to these colloidal brushes. The α-helix and β-sheet content of the proteins was nearly fully retained in the adsorbed state for all systems. Only in the case of BSA interacting with poly(styrenesulfonic) brushes could a slight loss of α-helix structure be observed. As the interaction of SPB and proteins can be controlled by the ionic strength in the buffer, additional experiments were performed to release the adsorbed protein. The amount of released protein was quantified and was found to be strongly dependent on the kind of protein and brush used. The secondary structure of the released proteins could be analyzed as well. An almost full preservation of secondary structure was found. This demonstrates that SPB are well-suited to immobilize proteins. The SPB can be charged and decharged under retention of the secondary structure of the biomolecules.

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ISO 690WITTEMANN, Alexander, Matthias BALLAUFF, 2004. Secondary structure analysis of proteins embedded in spherical polyelectrolyte brushes by FT-IR spectroscopy. In: Analytical Chemistry. 2004, 76(10), pp. 2813-2819. ISSN 0003-2700. Available under: doi: 10.1021/ac0354692
BibTex
@article{Wittemann2004-05-15Secon-20217,
  year={2004},
  doi={10.1021/ac0354692},
  title={Secondary structure analysis of proteins embedded in spherical polyelectrolyte brushes by FT-IR spectroscopy},
  number={10},
  volume={76},
  issn={0003-2700},
  journal={Analytical Chemistry},
  pages={2813--2819},
  author={Wittemann, Alexander and Ballauff, Matthias}
}
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    <dcterms:abstract xml:lang="eng">The adsorption of bovine serum albumin (BSA), bovine β-lactoglobulin, and bovine pancreatic ribonuclease A onto spherical polyelectrolyte brushes (SPB) is reported. The SPB consist of narrowly distributed poly(styrene) core particles (diameter 100 nm) onto which linear chains of anionic polyelectrolytes are grafted. The polyelectrolyte shell consists of either the weak polyelectrolyte poly(acrylic acid) or the strong polyacid poly(styrenesulfonate). The SPB particles are dispersed in H2O at room temperature. The secondary structure of the proteins was investigated by Fourier transform infrared spectroscopy in transmission mode before and during adsorption to these colloidal brushes. The α-helix and β-sheet content of the proteins was nearly fully retained in the adsorbed state for all systems. Only in the case of BSA interacting with poly(styrenesulfonic) brushes could a slight loss of α-helix structure be observed. As the interaction of SPB and proteins can be controlled by the ionic strength in the buffer, additional experiments were performed to release the adsorbed protein. The amount of released protein was quantified and was found to be strongly dependent on the kind of protein and brush used. The secondary structure of the released proteins could be analyzed as well. An almost full preservation of secondary structure was found. This demonstrates that SPB are well-suited to immobilize proteins. The SPB can be charged and decharged under retention of the secondary structure of the biomolecules.</dcterms:abstract>
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