Protein Resistance Driven by Polymer Nanoarchitecture

Maya K. Endoh; Yuma Morimitsu; Daniel Salatto; Zhixing Huang; Mani Sen; Weiyi Li; Yizhi Meng; David G. Thanassi; Jan Michael Y. Carrillo; Bobby G. Sumpter; Daisuke Kawaguchi; Keiji Tanaka; Tadanori Koga

doi:10.1021/acsmacrolett.9b00518

Protein Resistance Driven by Polymer Nanoarchitecture

Maya K. Endoh, Yuma Morimitsu, Daniel Salatto, Zhixing Huang, Mani Sen, Weiyi Li, Yizhi Meng, David G. Thanassi, Jan Michael Y. Carrillo, Bobby G. Sumpter, Daisuke Kawaguchi, Keiji Tanaka, Tadanori Koga

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Abstract

We report that the nanometer-scale architecture of polymer chains plays a crucial role in its protein resistant property over surface chemistry. Protein-repellent (noncharged), few nanometer thick polymer layers were designed with homopolymer chains physisorbed on solids. We evaluated the antifouling property of the hydrophilic or hydrophobic adsorbed homopolymer chains against bovine serum albumin in water. Molecular dynamics simulations along with sum frequency generation spectroscopy data revealed the self-organized nanoarchitecture of the adsorbed chains composed of inner nematic-like ordered segments and outer brush-like segments across homopolymer systems with different interactions among a polymer, substrate, and interfacial water. We propose that this structure acts as a dual barrier against protein adsorption.

Original language	English
Pages (from-to)	1153-1159
Number of pages	7
Journal	ACS Macro Letters
Volume	8
Issue number	9
DOIs	https://doi.org/10.1021/acsmacrolett.9b00518
State	Published - Sep 17 2019

Funding

We thank Ruipeng Li and Masafumi Fukuto for the SAXS and XR experiments and Dmytro Nykypanchuk for the photon counting spectrofluorometer experiments. T. Koga and M. K. Endoh acknowledge financial support from Kuraray. This research used resources of the Center for Functional Nanomaterials and the National Synchrotron Light Source II, which are U.S. DOE Office of Science Facilities, at Brookhaven National Laboratory under Contract DE-SC0012704. The computational/simulations aspect of this work was performed at the Center for Nanophase Materials Sciences, a U.S. Department of Energy Office of Science User Facility. This research also used resources of the Oak Ridge Leadership Computing Facility, which is a DOE Office of Science User Facility supported under Contract DE-AC05-00OR22725.

Funders	Funder number
National Synchrotron Light Source II
U.S. Department of Energy
Office of Science	DE-AC05-00OR22725
Brookhaven National Laboratory	DE-SC0012704
Japan Society for the Promotion of Science	17J00917

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title = "Protein Resistance Driven by Polymer Nanoarchitecture",

abstract = "We report that the nanometer-scale architecture of polymer chains plays a crucial role in its protein resistant property over surface chemistry. Protein-repellent (noncharged), few nanometer thick polymer layers were designed with homopolymer chains physisorbed on solids. We evaluated the antifouling property of the hydrophilic or hydrophobic adsorbed homopolymer chains against bovine serum albumin in water. Molecular dynamics simulations along with sum frequency generation spectroscopy data revealed the self-organized nanoarchitecture of the adsorbed chains composed of inner nematic-like ordered segments and outer brush-like segments across homopolymer systems with different interactions among a polymer, substrate, and interfacial water. We propose that this structure acts as a dual barrier against protein adsorption.",

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AU - Endoh, Maya K.

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AU - Li, Weiyi

AU - Meng, Yizhi

AU - Thanassi, David G.

AU - Carrillo, Jan Michael Y.

AU - Sumpter, Bobby G.

AU - Kawaguchi, Daisuke

AU - Tanaka, Keiji

AU - Koga, Tadanori

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AB - We report that the nanometer-scale architecture of polymer chains plays a crucial role in its protein resistant property over surface chemistry. Protein-repellent (noncharged), few nanometer thick polymer layers were designed with homopolymer chains physisorbed on solids. We evaluated the antifouling property of the hydrophilic or hydrophobic adsorbed homopolymer chains against bovine serum albumin in water. Molecular dynamics simulations along with sum frequency generation spectroscopy data revealed the self-organized nanoarchitecture of the adsorbed chains composed of inner nematic-like ordered segments and outer brush-like segments across homopolymer systems with different interactions among a polymer, substrate, and interfacial water. We propose that this structure acts as a dual barrier against protein adsorption.

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Protein Resistance Driven by Polymer Nanoarchitecture

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