title: Solid-solid interface adsorption of proteins and enzymes in nanophase-separated amphiphilic conetworks.
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.
authors.affiliation: Chair of Biomaterials and Polymer Science, Department of Bio- and Chemical Engineering, TU Dortmund, Dortmund, Germany.
authors.forename: Stephan
authors.initials: S
authors.lastname: Dech
authors.forename: Tobias
authors.initials: T
authors.lastname: Cramer
authors.forename: Reinhild
authors.initials: R
authors.lastname: Ladisch
authors.forename: Nico
authors.initials: N
authors.lastname: Bruns
authors.forename: Joerg C
authors.initials: JC
authors.lastname: Tiller
mesh_terms: D000327:Adsorption; D004797:Enzyme-Linked Immunosorbent Assay; D004798:Enzymes / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011506:Proteins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013499:Surface Properties
chemical_list: D004798:Enzymes; D011506:Proteins