Investigation of the hydration of nonfouling material poly(sulfobetaine methacrylate) by low-field nuclear magnetic resonance

The strong surface hydration layer of nonfouling materials plays a key role in their resistance to nonspecific protein adsorption. Poly(sulfobetaine methacrylate) (polySBMA) is an effective material that can resist nonspecific protein adsorption and cell adhesion. About eight water molecules are tig...

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Publié dans:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 28(2012), 19 vom: 15. Mai, Seite 7436-41
Auteur principal: Wu, Jiang (Auteur)
Autres auteurs: Lin, Weifeng, Wang, Zhen, Chen, Shengfu, Chang, Yung
Format: Article en ligne
Langue:English
Publié: 2012
Accès à la collection:Langmuir : the ACS journal of surfaces and colloids
Sujets:Journal Article Research Support, Non-U.S. Gov't Methacrylates sulfobetaine methacrylate polymer Betaine 3SCV180C9W sulfobetaine 8CVU22OCJW
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520 |a The strong surface hydration layer of nonfouling materials plays a key role in their resistance to nonspecific protein adsorption. Poly(sulfobetaine methacrylate) (polySBMA) is an effective material that can resist nonspecific protein adsorption and cell adhesion. About eight water molecules are tightly bound with one sulfobetaine (SB) unit, and additional water molecules over 8:1 ratio mainly swell the polySBMA matrix, which is obtained through the measurement of T(2) relaxation time by low-field nuclear magnetic resonance (LF-NMR). This result was also supported by the endothermic behavior of water/polySBMA mixtures measured by differential scanning calorimetry (DSC). Furthermore, by comparing both results of polySBMA and poly(ethylene glycol) (PEG), it is found that (1) the hydrated water molecules on the SB unit are more tightly bound than on the ethylene glycol (EG) unit before saturation, and (2) the additional water molecules after forming the hydration layer in polySBMA solutions show higher freedom than those in PEG. These results might illustrate the reason for higher resistance of zwitterionic materials to nonspecific protein adsorptions compared to that of PEGs 
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700 1 |a Lin, Weifeng  |e verfasserin  |4 aut 
700 1 |a Wang, Zhen  |e verfasserin  |4 aut 
700 1 |a Chen, Shengfu  |e verfasserin  |4 aut 
700 1 |a Chang, Yung  |e verfasserin  |4 aut 
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