Final published version
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Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Highly Active Protein Surfaces Enabled by Plant-Based Polyphenol Coatings
AU - Sousa, Ana M. L.
AU - Li, Tai-De
AU - Varghese, Sabu
AU - Halling, Peter J.
AU - Aaron Lau, King Hang
PY - 2018/11/14
Y1 - 2018/11/14
N2 - Proteins represent complex biomolecules capable of wide-ranging but also highly specific functionalities. Their immobilization on material supports can enable broad applications from sensing and industrial biocatalysis to biomedical interfaces and materials. We demonstrate the advantages of using aqueous-processed cross-linked polyphenol coatings for immobilizing proteins, including IgG, avidin, and various single and multidomain enzymes on diverse materials, to enable active biofunctional structures (e.g., ca. 2.2, 1.7, 1.1, and 4.8 mg·m-2 active phosphatase on nanoporous cellulose and alumina, steel mesh, and polyester fabric, respectively). Enzyme assays, X-ray photoelectron spectroscopy, silver staining, supplemented with contact angle, solid-state 13C NMR, HPLC, and ESI-MS measurements were used to characterize the polyphenols, coatings, and protein layers. We show that the functionalization process may be advantageously optimized directly for protein activity rather than the traditional focus on the thickness of the coating layer. Higher activities (by more than an order of magnitude in some cases) and wider process pH and material compatibility are demonstrated with polyphenol coatings than other approaches such as polydopamine. Coatings formed from different plant polyphenol extracts, even at lowered purity (and cost), were also found to be highly functional. Chemically, our results indicate that polyphenol coatings differ from polydopamine mainly because of the elimination of amine groups, and that polyphenol layers with intermediate levels of reactivity may better lead to high immobilized protein activity. Overall, an improved understanding of simple-to-use polyphenol coatings has been obtained, which enabled a significant development in active protein surfaces that may be applied across diverse materials and nanostructured supports. © 2018 American Chemical Society.
AB - Proteins represent complex biomolecules capable of wide-ranging but also highly specific functionalities. Their immobilization on material supports can enable broad applications from sensing and industrial biocatalysis to biomedical interfaces and materials. We demonstrate the advantages of using aqueous-processed cross-linked polyphenol coatings for immobilizing proteins, including IgG, avidin, and various single and multidomain enzymes on diverse materials, to enable active biofunctional structures (e.g., ca. 2.2, 1.7, 1.1, and 4.8 mg·m-2 active phosphatase on nanoporous cellulose and alumina, steel mesh, and polyester fabric, respectively). Enzyme assays, X-ray photoelectron spectroscopy, silver staining, supplemented with contact angle, solid-state 13C NMR, HPLC, and ESI-MS measurements were used to characterize the polyphenols, coatings, and protein layers. We show that the functionalization process may be advantageously optimized directly for protein activity rather than the traditional focus on the thickness of the coating layer. Higher activities (by more than an order of magnitude in some cases) and wider process pH and material compatibility are demonstrated with polyphenol coatings than other approaches such as polydopamine. Coatings formed from different plant polyphenol extracts, even at lowered purity (and cost), were also found to be highly functional. Chemically, our results indicate that polyphenol coatings differ from polydopamine mainly because of the elimination of amine groups, and that polyphenol layers with intermediate levels of reactivity may better lead to high immobilized protein activity. Overall, an improved understanding of simple-to-use polyphenol coatings has been obtained, which enabled a significant development in active protein surfaces that may be applied across diverse materials and nanostructured supports. © 2018 American Chemical Society.
KW - biointerface
KW - enzyme biocatalysis
KW - polydopamine
KW - polyphenol
KW - protein immobilization
KW - Alumina
KW - Aluminum oxide
KW - Biocatalysts
KW - Catalysis
KW - Contact angle
KW - Enzyme immobilization
KW - X ray photoelectron spectroscopy
KW - Biointerfaces
KW - Enzyme biocatalysis
KW - Polydopamine
KW - Polyphenols
KW - Protein immobilization
KW - Coatings
U2 - 10.1021/acsami.8b13793
DO - 10.1021/acsami.8b13793
M3 - Journal article
VL - 10
SP - 39353
EP - 39362
JO - ACS Applied Materials and Interfaces
JF - ACS Applied Materials and Interfaces
SN - 1944-8244
IS - 45
ER -