Surface-grafted polysarcosine as a peptoid antifouling polymer brush

K. H. A. Lau, C. L. Ren, T. S. Sileika, S. H. Park, I. Szleifer, P. B. Messersmith

Research output: Contribution to journalArticle

93 Citations (Scopus)
170 Downloads (Pure)

Abstract

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.
Original languageEnglish
Pages (from-to)16099-16107
Number of pages9
JournalLangmuir
Volume28
Issue number46
Early online date26 Oct 2012
DOIs
Publication statusPublished - 2012

Fingerprint

Peptoids
antifouling
brushes
Brushes
Polymers
Proteins
Chain length
polymers
Adsorption
proteins
attachment
Amino acids
adsorption
glycine
High pressure liquid chromatography
Sarcosine
Biomolecules
Fibroblasts
Angle measurement
Density (specific gravity)

Keywords

  • chain-length
  • self-assembled
  • monolayers
  • protein
  • adsorption
  • pseudomonas-aeruginosa
  • competitive
  • nosocomial
  • infections
  • poly(ethylene oxide)
  • platelet-adhesion
  • plasma-proteins
  • titanium-oxide

Cite this

Lau, K. H. A., Ren, C. L., Sileika, T. S., Park, S. H., Szleifer, I., & Messersmith, P. B. (2012). Surface-grafted polysarcosine as a peptoid antifouling polymer brush. Langmuir, 28(46), 16099-16107. https://doi.org/10.1021/la302131n
Lau, K. H. A. ; Ren, C. L. ; Sileika, T. S. ; Park, S. H. ; Szleifer, I. ; Messersmith, P. B. / Surface-grafted polysarcosine as a peptoid antifouling polymer brush. In: Langmuir. 2012 ; Vol. 28, No. 46. pp. 16099-16107.
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abstract = "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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Lau, KHA, Ren, CL, Sileika, TS, Park, SH, Szleifer, I & Messersmith, PB 2012, 'Surface-grafted polysarcosine as a peptoid antifouling polymer brush', Langmuir, vol. 28, no. 46, pp. 16099-16107. https://doi.org/10.1021/la302131n

Surface-grafted polysarcosine as a peptoid antifouling polymer brush. / Lau, K. H. A.; Ren, C. L.; Sileika, T. S.; Park, S. H.; Szleifer, I.; Messersmith, P. B.

In: Langmuir, Vol. 28, No. 46, 2012, p. 16099-16107.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Surface-grafted polysarcosine as a peptoid antifouling polymer brush

AU - Lau, K. H. A.

AU - Ren, C. L.

AU - Sileika, T. S.

AU - Park, S. H.

AU - Szleifer, I.

AU - Messersmith, P. B.

PY - 2012

Y1 - 2012

N2 - 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.

AB - 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.

KW - chain-length

KW - self-assembled

KW - monolayers

KW - protein

KW - adsorption

KW - pseudomonas-aeruginosa

KW - competitive

KW - nosocomial

KW - infections

KW - poly(ethylene oxide)

KW - platelet-adhesion

KW - plasma-proteins

KW - titanium-oxide

UR - http://pubs.acs.org/journal/langd5

U2 - 10.1021/la302131n

DO - 10.1021/la302131n

M3 - Article

VL - 28

SP - 16099

EP - 16107

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 46

ER -

Lau KHA, Ren CL, Sileika TS, Park SH, Szleifer I, Messersmith PB. Surface-grafted polysarcosine as a peptoid antifouling polymer brush. Langmuir. 2012;28(46):16099-16107. https://doi.org/10.1021/la302131n