Solid-solid interface adsorption of proteins and enzymes in nanophase-separated amphiphilic conetworks

Stephan Dech, Tobias Cramer, Reinhild Ladisch, Nico Bruns, Joerg C. Tiller

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Amphiphilic polymer conetworks (APCNs) are materials with a very large interface between their hydrophilic and hydrophobic phases due to their nanophase-separated morphologies. Proteins were found to enrich in APCNs by up to 2 orders of magnitude when incubated in aqueous protein solutions, raising the question of the driving force of protein uptake into APCNs. The loading of poly(2-hydroxyethyl acrylate)-linked by-poly(dimethylsiloxane) (PHEA-l-PDMS) with heme proteins (myoglobin, horseradish peroxidase, hemoglobin) and lipases was studied under variation of parameters such as incubation time, pH, concentration of the protein solution, and conetwork composition. Adsorption of enzymes to the uncharged interface is the main reason for protein uptake, resulting in protein loading of up to 23 wt %. Experimental results were supported by computation of electrostatic potential maps of a lipase, indicating that hydrophobic patches are responsible for the adsorption to the interface. The findings underscore the potential of enzyme-loaded APCNs in biocatalysis and as sensors.

LanguageEnglish
Pages1594-1601
Number of pages8
JournalBiomacromolecules
Volume12
Issue number5
DOIs
Publication statusPublished - 9 May 2011

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Enzymes
Proteins
Adsorption
Polymers
Lipases
Lipase
Hemeproteins
Myoglobin
Hemoglobin
Polydimethylsiloxane
Horseradish Peroxidase
Electrostatics
Hemoglobins
Sensors
Chemical analysis

Keywords

  • amphiphilic polymer conetworks
  • nanophase-separated morphologies
  • heme proteins

Cite this

Dech, Stephan ; Cramer, Tobias ; Ladisch, Reinhild ; Bruns, Nico ; Tiller, Joerg C. / Solid-solid interface adsorption of proteins and enzymes in nanophase-separated amphiphilic conetworks. In: Biomacromolecules. 2011 ; Vol. 12, No. 5. pp. 1594-1601.
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Solid-solid interface adsorption of proteins and enzymes in nanophase-separated amphiphilic conetworks. / Dech, Stephan; Cramer, Tobias; Ladisch, Reinhild; Bruns, Nico; Tiller, Joerg C.

In: Biomacromolecules, Vol. 12, No. 5, 09.05.2011, p. 1594-1601.

Research output: Contribution to journalArticle

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