Protein Adsorption and Coordination-Based End-Tethering of Functional Polymers on Metal-Phenolic Network Films

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Protein Adsorption and Coordination-Based End-Tethering of Functional Polymers on Metal-Phenolic Network Films. / Tardy, Blaise L.; Richardson, Joseph J.; Nithipipat, Vichida; Kempe, Kristian; Guo, Junling; Cho, Kwun Lun; Rahim, Md Arifur; Ejima, Hirotaka; Caruso, Frank.

julkaisussa: Biomacromolecules, Vuosikerta 20, Nro 3, 11.03.2019, s. 1421-1428.

Tutkimustuotos: Lehtiartikkelivertaisarvioitu

Harvard

Tardy, BL, Richardson, JJ, Nithipipat, V, Kempe, K, Guo, J, Cho, KL, Rahim, MA, Ejima, H & Caruso, F 2019, 'Protein Adsorption and Coordination-Based End-Tethering of Functional Polymers on Metal-Phenolic Network Films', Biomacromolecules, Vuosikerta. 20, Nro 3, Sivut 1421-1428. https://doi.org/10.1021/acs.biomac.9b00006

APA

Vancouver

Author

Tardy, Blaise L. ; Richardson, Joseph J. ; Nithipipat, Vichida ; Kempe, Kristian ; Guo, Junling ; Cho, Kwun Lun ; Rahim, Md Arifur ; Ejima, Hirotaka ; Caruso, Frank. / Protein Adsorption and Coordination-Based End-Tethering of Functional Polymers on Metal-Phenolic Network Films. Julkaisussa: Biomacromolecules. 2019 ; Vuosikerta 20, Nro 3. Sivut 1421-1428.

Bibtex - Lataa

@article{568c211834f548ecbdd924ad17d16e29,
title = "Protein Adsorption and Coordination-Based End-Tethering of Functional Polymers on Metal-Phenolic Network Films",
abstract = "Metal-phenolic network (MPN) coatings have generated increasing interest owing to their biologically inspired nature, facile fabrication, and near-universal adherence, especially for biomedical applications. However, a key issue in biomedicine is protein fouling, and the adsorption of proteins on tannic acid-based MPNs remains to be comprehensively studied. Herein, we investigate the interaction of specific biomedically relevant proteins in solution (e.g., bovine serum albumin (BSA), immunoglobulin G (IgG), fibrinogen) and complex biological media (serum) using layer-by-layer-assembled tannic acid/Fe III MPN films. When Fe III was the outermost layer, galloyl-modified poly(2-ethyl-2-oxazoline) (P(EtOx)-Gal) could be grafted to the films through coordination bonds. Protein fouling and bacterial adhesion were greatly suppressed after functionalization with P(EtOx)-Gal and the mass of adsorbed protein was reduced by 79{\%}. Interestingly, larger proteins adsorbed more on both the MPNs and P(EtOx)-functionalized MPNs. This study provides fundamental information on the interactions of MPNs with single proteins, mixtures of proteins as encountered in serum, and the noncovalent, coordination-based, functionalization of MPN films.",
author = "Tardy, {Blaise L.} and Richardson, {Joseph J.} and Vichida Nithipipat and Kristian Kempe and Junling Guo and Cho, {Kwun Lun} and Rahim, {Md Arifur} and Hirotaka Ejima and Frank Caruso",
year = "2019",
month = "3",
day = "11",
doi = "10.1021/acs.biomac.9b00006",
language = "English",
volume = "20",
pages = "1421--1428",
journal = "Biomacromolecules",
issn = "1525-7797",
publisher = "AMERICAN CHEMICAL SOCIETY",
number = "3",

}

RIS - Lataa

TY - JOUR

T1 - Protein Adsorption and Coordination-Based End-Tethering of Functional Polymers on Metal-Phenolic Network Films

AU - Tardy, Blaise L.

AU - Richardson, Joseph J.

AU - Nithipipat, Vichida

AU - Kempe, Kristian

AU - Guo, Junling

AU - Cho, Kwun Lun

AU - Rahim, Md Arifur

AU - Ejima, Hirotaka

AU - Caruso, Frank

PY - 2019/3/11

Y1 - 2019/3/11

N2 - Metal-phenolic network (MPN) coatings have generated increasing interest owing to their biologically inspired nature, facile fabrication, and near-universal adherence, especially for biomedical applications. However, a key issue in biomedicine is protein fouling, and the adsorption of proteins on tannic acid-based MPNs remains to be comprehensively studied. Herein, we investigate the interaction of specific biomedically relevant proteins in solution (e.g., bovine serum albumin (BSA), immunoglobulin G (IgG), fibrinogen) and complex biological media (serum) using layer-by-layer-assembled tannic acid/Fe III MPN films. When Fe III was the outermost layer, galloyl-modified poly(2-ethyl-2-oxazoline) (P(EtOx)-Gal) could be grafted to the films through coordination bonds. Protein fouling and bacterial adhesion were greatly suppressed after functionalization with P(EtOx)-Gal and the mass of adsorbed protein was reduced by 79%. Interestingly, larger proteins adsorbed more on both the MPNs and P(EtOx)-functionalized MPNs. This study provides fundamental information on the interactions of MPNs with single proteins, mixtures of proteins as encountered in serum, and the noncovalent, coordination-based, functionalization of MPN films.

AB - Metal-phenolic network (MPN) coatings have generated increasing interest owing to their biologically inspired nature, facile fabrication, and near-universal adherence, especially for biomedical applications. However, a key issue in biomedicine is protein fouling, and the adsorption of proteins on tannic acid-based MPNs remains to be comprehensively studied. Herein, we investigate the interaction of specific biomedically relevant proteins in solution (e.g., bovine serum albumin (BSA), immunoglobulin G (IgG), fibrinogen) and complex biological media (serum) using layer-by-layer-assembled tannic acid/Fe III MPN films. When Fe III was the outermost layer, galloyl-modified poly(2-ethyl-2-oxazoline) (P(EtOx)-Gal) could be grafted to the films through coordination bonds. Protein fouling and bacterial adhesion were greatly suppressed after functionalization with P(EtOx)-Gal and the mass of adsorbed protein was reduced by 79%. Interestingly, larger proteins adsorbed more on both the MPNs and P(EtOx)-functionalized MPNs. This study provides fundamental information on the interactions of MPNs with single proteins, mixtures of proteins as encountered in serum, and the noncovalent, coordination-based, functionalization of MPN films.

UR - http://www.scopus.com/inward/record.url?scp=85062690872&partnerID=8YFLogxK

U2 - 10.1021/acs.biomac.9b00006

DO - 10.1021/acs.biomac.9b00006

M3 - Article

C2 - 30794387

AN - SCOPUS:85062690872

VL - 20

SP - 1421

EP - 1428

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1525-7797

IS - 3

ER -

ID: 32664390