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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.

Authors:
 [1];  [2];  [1];  [1];  [1];  [1];  [1];  [3]; ORCiD logo [4]; ORCiD logo [4]; ORCiD logo [5]; ORCiD logo [5]; ORCiD logo [6]
  1. Stony Brook Univ., NY (United States). Dept. of Materials Science and Chemical Engineering
  2. Stony Brook Univ., NY (United States). Dept. of Materials Science and Chemical Engineering; Kyushu Univ., Fukuoka (Japan)
  3. Stony Brook Univ., NY (United States). Dept. of Molecular Genetics & Microbiology and Center for Infectious Diseases
  4. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Nanophase Materials Sciences and Computational Sciences and Engineering Division
  5. Kyushu Univ., Fukuoka (Japan)
  6. Stony Brook Univ., NY (United States). Dept. of Materials Science and Chemical Engineering, and Dept. of Chemistry
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
OSTI Identifier:
1559683
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
ACS Macro Letters
Additional Journal Information:
Journal Volume: 8; Journal Issue: N/A; Journal ID: ISSN 2161-1653
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE

Citation Formats

Endoh, Maya K., Morimitsu, Yuma, Salatto, Daniel, Huang, Zhixing, Sen, Mani, Li, Weiyi, Meng, Yizhi, Thanassi, David G., Carrillo, Jan-Michael Y., Sumpter, Bobby G., Kawaguchi, Daisuke, Tanaka, Keiji, and Koga, Tadanori. Protein Resistance Driven by Polymer Nanoarchitecture. United States: N. p., 2019. Web. doi:10.1021/acsmacrolett.9b00518.
Endoh, Maya K., Morimitsu, Yuma, Salatto, Daniel, Huang, Zhixing, Sen, Mani, Li, Weiyi, Meng, Yizhi, Thanassi, David G., Carrillo, Jan-Michael Y., Sumpter, Bobby G., Kawaguchi, Daisuke, Tanaka, Keiji, & Koga, Tadanori. Protein Resistance Driven by Polymer Nanoarchitecture. United States. https://doi.org/10.1021/acsmacrolett.9b00518
Endoh, Maya K., Morimitsu, Yuma, Salatto, Daniel, Huang, Zhixing, Sen, Mani, Li, Weiyi, Meng, Yizhi, Thanassi, David G., Carrillo, Jan-Michael Y., Sumpter, Bobby G., Kawaguchi, Daisuke, Tanaka, Keiji, and Koga, Tadanori. Thu . "Protein Resistance Driven by Polymer Nanoarchitecture". United States. https://doi.org/10.1021/acsmacrolett.9b00518. https://www.osti.gov/servlets/purl/1559683.
@article{osti_1559683,
title = {Protein Resistance Driven by Polymer Nanoarchitecture},
author = {Endoh, Maya K. and Morimitsu, Yuma and Salatto, Daniel and Huang, Zhixing and Sen, Mani and Li, Weiyi and Meng, Yizhi and Thanassi, David G. and Carrillo, Jan-Michael Y. and Sumpter, Bobby G. and Kawaguchi, Daisuke and Tanaka, Keiji and Koga, Tadanori},
abstractNote = {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.},
doi = {10.1021/acsmacrolett.9b00518},
journal = {ACS Macro Letters},
number = N/A,
volume = 8,
place = {United States},
year = {Thu Aug 22 00:00:00 EDT 2019},
month = {Thu Aug 22 00:00:00 EDT 2019}
}

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