Details
| Original language | English |
|---|---|
| Pages (from-to) | 899-906 |
| Number of pages | 8 |
| Journal | Molecular Simulation |
| Volume | 37 |
| Issue number | 11 |
| Early online date | 26 Aug 2011 |
| Publication status | Published - Sept 2011 |
| Externally published | Yes |
Abstract
The non-specific adsorption of proteins on surfaces is a well-known and mostly undesirable phenomena, which is reduced by a surface coating with the linear polyether poly(ethylene glycol) (PEG) as the current benchmark material. However, the molecular mechanism of protein-resistant surfaces is still not fully understood. Two main hypotheses are generally applied. The first one is steric repulsion of the highly flexible tethered polymer chains, leading to an entropic penalty by adsorption of proteins due to the reduction in polymer chain mobility. The second one argues with well-hydrated polymer chains generating a repulsive interfacial water layer. In this article, we compare the three different protein-resistant polyether structures PEG, linear polyglycerol (LPG(OH)) and linear poly(methyl glycerol) (LPG(OMe)) to get new insights into the molecular mechanism behind protein resistance. In a theoretical approach, we apply an entropy estimator that assesses the conformational states of the tethered polyethers from MD simulations. It reveals the entropy differences between these polyethers to be in the order PEG > LPG(OH) > LPG(OMe). Moreover, experiments on fibrinogen adsorption of these surfaces via surface plasmon resonance spectroscopy are performed and correlated with the theoretical studies. We find that protein resistant properties of surfaces are likely to arise from an interplay of different factors.
Keywords
- entropy estimation, MD simulation, polyethylene glycol, protein-resistant surfaces, SPR
ASJC Scopus subject areas
- Chemistry(all)
- General Chemistry
- Computer Science(all)
- Information Systems
- Mathematics(all)
- Modelling and Simulation
- Chemical Engineering(all)
- General Chemical Engineering
- Materials Science(all)
- General Materials Science
- Physics and Astronomy(all)
- Condensed Matter Physics
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In: Molecular Simulation, Vol. 37, No. 11, 09.2011, p. 899-906.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Computational entropy estimation of linear polyether-modified surfaces and correlation with protein resistant properties of such surfaces
AU - Weber, Marcus
AU - Bujotzek, Alexander
AU - Andrae, Karsten
AU - Weinhart, Marie
AU - Haag, Rainer
PY - 2011/9
Y1 - 2011/9
N2 - The non-specific adsorption of proteins on surfaces is a well-known and mostly undesirable phenomena, which is reduced by a surface coating with the linear polyether poly(ethylene glycol) (PEG) as the current benchmark material. However, the molecular mechanism of protein-resistant surfaces is still not fully understood. Two main hypotheses are generally applied. The first one is steric repulsion of the highly flexible tethered polymer chains, leading to an entropic penalty by adsorption of proteins due to the reduction in polymer chain mobility. The second one argues with well-hydrated polymer chains generating a repulsive interfacial water layer. In this article, we compare the three different protein-resistant polyether structures PEG, linear polyglycerol (LPG(OH)) and linear poly(methyl glycerol) (LPG(OMe)) to get new insights into the molecular mechanism behind protein resistance. In a theoretical approach, we apply an entropy estimator that assesses the conformational states of the tethered polyethers from MD simulations. It reveals the entropy differences between these polyethers to be in the order PEG > LPG(OH) > LPG(OMe). Moreover, experiments on fibrinogen adsorption of these surfaces via surface plasmon resonance spectroscopy are performed and correlated with the theoretical studies. We find that protein resistant properties of surfaces are likely to arise from an interplay of different factors.
AB - The non-specific adsorption of proteins on surfaces is a well-known and mostly undesirable phenomena, which is reduced by a surface coating with the linear polyether poly(ethylene glycol) (PEG) as the current benchmark material. However, the molecular mechanism of protein-resistant surfaces is still not fully understood. Two main hypotheses are generally applied. The first one is steric repulsion of the highly flexible tethered polymer chains, leading to an entropic penalty by adsorption of proteins due to the reduction in polymer chain mobility. The second one argues with well-hydrated polymer chains generating a repulsive interfacial water layer. In this article, we compare the three different protein-resistant polyether structures PEG, linear polyglycerol (LPG(OH)) and linear poly(methyl glycerol) (LPG(OMe)) to get new insights into the molecular mechanism behind protein resistance. In a theoretical approach, we apply an entropy estimator that assesses the conformational states of the tethered polyethers from MD simulations. It reveals the entropy differences between these polyethers to be in the order PEG > LPG(OH) > LPG(OMe). Moreover, experiments on fibrinogen adsorption of these surfaces via surface plasmon resonance spectroscopy are performed and correlated with the theoretical studies. We find that protein resistant properties of surfaces are likely to arise from an interplay of different factors.
KW - entropy estimation
KW - MD simulation
KW - polyethylene glycol
KW - protein-resistant surfaces
KW - SPR
UR - http://www.scopus.com/inward/record.url?scp=80052335669&partnerID=8YFLogxK
U2 - 10.1080/08927022.2011.566606
DO - 10.1080/08927022.2011.566606
M3 - Article
AN - SCOPUS:80052335669
VL - 37
SP - 899
EP - 906
JO - Molecular Simulation
JF - Molecular Simulation
SN - 0892-7022
IS - 11
ER -