Temperature-Activated PEG Surface Segregation Controls the Protein Repellency of Polymers

Murthy, N. Sanjeeva; Wang, Wenjie; Sommerfeld, Sven D.; Vaknin, David; Kohn, Joachim

doi:10.1021/acs.langmuir.9b00702

Title: Temperature-Activated PEG Surface Segregation Controls the Protein Repellency of Polymers

Abstract

Poly(ethylene glycol) (PEG) is widely used to modulate the hydration states of biomaterials and is often applied to produce nonfouling surfaces. Here, we present X-ray scattering data, which show that it is the surface segregation of PEG, not just its presence in the bulk, that makes this happen by influencing the hydrophilicity of PEG-containing substrates. We demonstrate a temperature-dependent trigger that transforms a PEG-containing substrate from a protein-adsorbing to a protein-repelling state. On films of poly(desaminotyrosyl-tyrosine-co-PEG carbonate) with high (20 wt %) PEG content, in which very little protein adsorption is expected, quartz crystal microbalance data showed significant adsorption of fibrinogen and bovine serum albumin at 8 °C. The surface became protein-repellent at 37.5 °C. When the same polymer was iodinated, the polymer was protein-adsorbent, even when 37 wt % PEG was incorporated into the polymer backbone. This demonstrates that high PEG content by itself is not sufficient to repel proteins. By inhibiting phase separation either with iodine or by lowering the temperature, we show that PEG must phase-separate and bloom to the surface to create an antifouling surface. Furthermore, these results suggest an opportunity to design materials with high PEG content that can be switched from a protein-attractant tomore »« less

Authors:

Murthy, N. Sanjeeva ^[1]; Wang, Wenjie ^[2]; Sommerfeld, Sven D. ^[3];

^[2];

^[2]

Rutgers - The State Univ. of New Jersey, Piscataway, NJ (United States)
Ames Lab. and Iowa State Univ., Ames, IA (United States)
Rutgers - The State Univ. of New Jersey, Piscataway, NJ (United States); Johns Hopkins Univ. School of Medicine, Baltimore, MD (United States)

Publication Date:: Sun Jun 30 00:00:00 EDT 2019

Research Org.:: Ames Lab., Ames, IA (United States)

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

OSTI Identifier:: 1560661

Report Number(s):: IS-J-10009
Journal ID: ISSN 0743-7463

Grant/Contract Number:: AC02-07CH11358; EB001046

Resource Type:: Accepted Manuscript

Journal Name:: Langmuir

Additional Journal Information:: Journal Volume: 35; Journal Issue: 30; Journal ID: ISSN 0743-7463

Publisher:: American Chemical Society

Country of Publication:: United States

Language:: English

Subject:: 36 MATERIALS SCIENCE

Citation Formats


                    Murthy, N. Sanjeeva, Wang, Wenjie, Sommerfeld, Sven D., Vaknin, David, and Kohn, Joachim. Temperature-Activated PEG Surface Segregation Controls the Protein Repellency of Polymers.  United States: N. p., 2019. 
Web.  doi:10.1021/acs.langmuir.9b00702.

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                    Murthy, N. Sanjeeva, Wang, Wenjie, Sommerfeld, Sven D., Vaknin, David, & Kohn, Joachim. Temperature-Activated PEG Surface Segregation Controls the Protein Repellency of Polymers.  United States.  https://doi.org/10.1021/acs.langmuir.9b00702

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                    Murthy, N. Sanjeeva, Wang, Wenjie, Sommerfeld, Sven D., Vaknin, David, and Kohn, Joachim. Sun .  
"Temperature-Activated PEG Surface Segregation Controls the Protein Repellency of Polymers".  United States.  https://doi.org/10.1021/acs.langmuir.9b00702.  https://www.osti.gov/servlets/purl/1560661.

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@article{osti_1560661,

  title        = {Temperature-Activated PEG Surface Segregation Controls the Protein Repellency of Polymers},

  author       = {Murthy, N. Sanjeeva and Wang, Wenjie and Sommerfeld, Sven D. and Vaknin, David and Kohn, Joachim},

  abstractNote = {Poly(ethylene glycol) (PEG) is widely used to modulate the hydration states of biomaterials and is often applied to produce nonfouling surfaces. Here, we present X-ray scattering data, which show that it is the surface segregation of PEG, not just its presence in the bulk, that makes this happen by influencing the hydrophilicity of PEG-containing substrates. We demonstrate a temperature-dependent trigger that transforms a PEG-containing substrate from a protein-adsorbing to a protein-repelling state. On films of poly(desaminotyrosyl-tyrosine-co-PEG carbonate) with high (20 wt %) PEG content, in which very little protein adsorption is expected, quartz crystal microbalance data showed significant adsorption of fibrinogen and bovine serum albumin at 8 °C. The surface became protein-repellent at 37.5 °C. When the same polymer was iodinated, the polymer was protein-adsorbent, even when 37 wt % PEG was incorporated into the polymer backbone. This demonstrates that high PEG content by itself is not sufficient to repel proteins. By inhibiting phase separation either with iodine or by lowering the temperature, we show that PEG must phase-separate and bloom to the surface to create an antifouling surface. Furthermore, these results suggest an opportunity to design materials with high PEG content that can be switched from a protein-attractant to a protein-repellent state by inducing phase separation through brief exposure to temperatures above their glass transition temperature.},

  doi          = {10.1021/acs.langmuir.9b00702},

  journal      = {Langmuir},

  number       = 30,

  volume       = 35,

  place        = {United States},

  year         = {Sun Jun 30 00:00:00 EDT 2019},

  month        = {Sun Jun 30 00:00:00 EDT 2019}

}

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Figure 1: Chemical structure of the PEG-containing tyrosine polycarbonates.

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