Surface-grafted polysarcosine as a peptoid antifouling polymer brush
Open accessAbstract
Poly(N-substituted glycine) "peptoids" are a class of peptidomimetic molecules receiving significant interest as engineered biomolecules. Sarcosine (i.e., poly(N-methyl glycine)) has the simplest side chain chemical structure of this family. In this Article, we demonstrate that surface-grafted polysarcosine (PSAR) brushes exhibit excellent resistance to nonspecific protein adsorption and cell attachment. Polysarcosine was coupled to a mussel adhesive protein-inspired DOPA-Lys pentapeptide, which enabled solution grafting and control of the surface chain density of the PSAR brushes. Protein adsorption was found to decrease monotonically with increasing grafted chain densities, and protein adsorption could be completely inhibited above certain critical chain densities specific to different polysarcosine chain lengths. The dependence of protein adsorption on chain length and density was also investigated by a molecular theory. PSAR brushes at high chain length and density were shown to resist fibroblast cell attachment over a 7 week period, as well as resist the attachment of some clinically relevant bacterial strains. The excellent antifouling performance of PSAR may be related to the highly hydrophilic character of polysarcosine, which was evident from high-pressure liquid chromatography measurements of polysarcosine and water contact angle measurements of the PSAR brushes. Peptoids have been shown to resist proteolytic degradation, and polysarcosine could be produced in large quantities by N-carboxy anhydride polymerization. In summary, surface-grafted polysarcosine peptoid brushes hold great promise for antifouling applications.
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Poly(sarcosine) has shown effective anti-fouling properties in recent studies.
“Among hydrophilic poly(amino acid)s, poly(sarcosine) has shown effective anti-fouling properties in recent studies [49, 94, 95].”
From Polymeric micelles for the delivery of poorly soluble drugs: From nanoformulation to clinical approval. (2020) · cites this paper as [95]
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- Authors
- Lau, K. H. A., Ren, C., Sileika, T. S., Park, S. H., Szleifer, I., & Messersmith, P. B.
- Affiliations
- Northwestern University (US)
- National Laboratory of Solid State Microstructures, Nanjing University, Nanjing 210093, China
- Corresponding author
- Szleifer, Igal
- Messersmith, Phillip B.
- Venue
- Langmuir
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-11-12
- Volume
- 28
- Issue
- 46
- Pages
- 16099-16107
- ISSN
- 0743-7463 (ISSN-L)
- 1520-5827
- PMC
- PMC3530414
- OpenAlex
- W2055162945
- Cited by
- 178
- References
- 75
- Citations by year
- 2026: 11 · 2025: 9 · 2024: 12 · 2023: 11 · 2022: 8 · 2021: 14 · 2020: 13 · 2019: 17 · 2018: 19 · 2017: 20 · 2016: 13 · 2015: 13 · 2014: 10 · 2013: 7
- FWCI
- 4.23
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Langmuir (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Strathprints: The University of Strathclyde institutional repository (University of Strathclyde) (submittedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL104966, F32HL104966)
- National Institute of Biomedical Imaging and Bioengineering (R01EB005772, EB005772)
- Topics
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Physical Sciences › Engineering › Ocean Engineering › Marine Biology and Environmental Chemistry
- Physical Sciences › Chemistry › Organic Chemistry › Advanced Polymer Synthesis and Characterization
- Keywords
- polysarcosine, peptoids, polymer brushes, antifouling surfaces, protein adsorption, cell attachment, mussel adhesive proteins, chain density, hydrophilicity, fibroblast adhesion, bacterial adhesion, surface grafting
- MeSH terms
- Adsorption, Animals, Bacterial Adhesion, Cell Adhesion, Escherichia coli, Fibroblasts, Materials Testing, Peptides, Proteins, Pseudomonas aeruginosa, Sarcosine, Staphylococcus epidermidis, Structure-Activity Relationship, Surface Properties, 3T3 Cells, Peptoids, Mice
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