Ionov, L. ; Synytska, A. ; Diez, S.
Protein-resistant polymer coatings based on surface-adsorbed poly(aminoethyl methacrylate)/poly(ethylene glycol) copolymers
We report on the protein-resistant properties of glass substrates coated with novel copolymers of 2-aminoethyl methacrylate hydrochloride and poly(ethylene glycol) methyl ether methacrylate (AEM-PEG). In comparison to currently available protein-blocking polymer systems, such as poly-l-lysine-poly(ethylene glycol), silane-based poly(ethylene glycol), and poly(ethylene glycol) brushes prepared by surface-initiated polymerization, the proposed AEM-PEG offers the combined advantages of low cost, simplicity of use, and applicability in aqueous solutions. We demonstrate the capability of AEM-PEG to block the surface binding of globular proteins (tubulin), their assemblies (microtubules), and functional motor proteins (kinesin-1). Moreover, we demonstrate the applicability of AEM-PEG for surface patterning of proteins in microfluidic devices.
Source
Biomacromolecules 11
Pages
233-237
DOI
http://dx.doi.org/10.1021/bm901082y
Published
January 2010
Protein-resistant polymer coatings based on surface-adsorbed poly(aminoethyl methacrylate)/poly(ethylene glycol) copolymers
We report on the protein-resistant properties of glass substrates coated with novel copolymers of 2-aminoethyl methacrylate hydrochloride and poly(ethylene glycol) methyl ether methacrylate (AEM-PEG). In comparison to currently available protein-blocking polymer systems, such as poly-l-lysine-poly(ethylene glycol), silane-based poly(ethylene glycol), and poly(ethylene glycol) brushes prepared by surface-initiated polymerization, the proposed AEM-PEG offers the combined advantages of low cost, simplicity of use, and applicability in aqueous solutions. We demonstrate the capability of AEM-PEG to block the surface binding of globular proteins (tubulin), their assemblies (microtubules), and functional motor proteins (kinesin-1). Moreover, we demonstrate the applicability of AEM-PEG for surface patterning of proteins in microfluidic devices.
Source
Biomacromolecules 11
Pages
233-237
DOI
http://dx.doi.org/10.1021/bm901082y
Published
January 2010
