Protein-induced changes in poly(ethylene glycol) brushes: Molecular weight and temperature dependence

N. V. Efremova, S. R. Sheth, Deborah E Leckband

Research output: Contribution to journalArticle

Abstract

Terminally grafted chains of poly(ethylene glycol) (PEG) and oligo(ethylene glycol) reduce protein adsorption and cell adhesion on material surfaces. However, previous studies showed that protein-PEG adhesion is induced by the application of pressure. Because polymer behavior can vary with the molecular weight, in this study we directly measured the forces between streptavidin and end-grafted monolayers of PEG of different molecular weights and at grafting densities. The results of these measurements show that grafted PEG chains can exist in two different states: a protein-repulsive state and a protein-attractive state. The attractive state can be induced not only by compression but also by increasing the temperature or by altering the polymer molecular weight. Both the critical applied load to induce the protein-attractive form of PEG and the relaxation time back to the protein-resistant state depend on the molecular weight of the grafted chains. The consequences of the observed behavior for the use of grafted PEG chains as protein antifouling coatings of biomaterials are discussed.

Original languageEnglish (US)
Pages (from-to)7628-7636
Number of pages9
JournalLangmuir
Volume17
Issue number24
DOIs
StatePublished - Nov 27 2001

Fingerprint

brushes
Brushes
Polyethylene glycols
glycols
molecular weight
ethylene
Molecular weight
proteins
Proteins
temperature dependence
Temperature
Polymers
adhesion
antifouling
Streptavidin
Ethylene Glycol
Cell adhesion
polymers
Biocompatible Materials
Ethylene glycol

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

Cite this

Protein-induced changes in poly(ethylene glycol) brushes : Molecular weight and temperature dependence. / Efremova, N. V.; Sheth, S. R.; Leckband, Deborah E.

In: Langmuir, Vol. 17, No. 24, 27.11.2001, p. 7628-7636.

Research output: Contribution to journalArticle

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