Protein Resistance Driven by Polymer Nanoarchitecture
- Stony Brook Univ., NY (United States). Dept. of Materials Science and Chemical Engineering
- Stony Brook Univ., NY (United States). Dept. of Materials Science and Chemical Engineering; Kyushu Univ., Fukuoka (Japan)
- Stony Brook Univ., NY (United States). Dept. of Molecular Genetics & Microbiology and Center for Infectious Diseases
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Nanophase Materials Sciences and Computational Sciences and Engineering Division
- Kyushu Univ., Fukuoka (Japan)
- Stony Brook Univ., NY (United States). Dept. of Materials Science and Chemical Engineering, and Dept. of Chemistry
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.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- AC05-00OR22725
- OSTI ID:
- 1559683
- Journal Information:
- ACS Macro Letters, Vol. 8, Issue N/A; ISSN 2161-1653
- Publisher:
- American Chemical Society (ACS)Copyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
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