Poly(L-lysine)-g-poly(ethylene glycol) layers on metal oxide surfaces: Attachment mechanism and effects of polymer architecture on resistance to protein adsorption

Gregory L. Kenausis, Janos Vörös, Donald L. Elbert, Ningping Huang, Rolf Hofer, Laurence Ruiz-Taylor, Marcus Textor, Jeffrey A. Hubbell, Nicholas D. Spencer

Research output: Contribution to journalArticlepeer-review

585 Scopus citations


The generation of surfaces and interfaces that are able to withstand protein adsorption is a major challenge in the design of blood-contacting materials for both medical implants and bioaffinity sensors. Poly(ethylene glycol)-derived materials are generally considered to be particularly effective candidates for the fabrication of protein-resistant materials. Most metallic biomaterials are covered by a protective, stable oxide film; converting such oxide surfaces, which are known to strongly interact with proteins, into noninteractive surfaces requires a specific design of the surface/interface architecture. A class of copolymers based on poly(L-lysine)-g-poly(ethylene glycol) (PLL-g-PEG) was found to spontaneously adsorb from aqueous solutions onto several metal oxide surfaces, such as TiO2, Si0.4Ti0.6O2, and Nb2O5, as measured by the in situ optical waveguide lightmode spectroscopy technique and by ex situ X-ray photoelectron spectroscopy. The resulting adsorbed layers are highly effective in reducing the adsorption both of blood serum and of individual proteins such as fibrinogen, which is known to play a major role in the cascade of events that lead to biomaterial-surface-induced blood coagulation and thrombosis. Adsorbed protein levels as low as <5 ng/cm2 could be achieved for an optimized polymer architecture. The modified surfaces are stable to desorption under flow conditions at 37 °C and pH 7.4 in HEPES [4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid] and PBS (phosphate-buffered saline) buffers. The adsorbed layer of copolymer is thought to form a comblike structure at the surface, with positively charged primary amine groups of the PLL bound to the negatively charged metal oxide surface, while the hydrophilic and uncharged PEG side chains are exposed to the solution phase. Copolymer architecture is an important factor in the resulting protein resistance; it is discussed on the basis of packing-density considerations and the corresponding radii of gyration of the different PEG chain lengths studied. This surface functionalization technology is believed to be of value for use in both the biomaterial and biosensor areas, as the chosen macromolecules are biocompatible and the application is straightforward and cost-effective.

Original languageEnglish (US)
Pages (from-to)3298-3309
Number of pages12
JournalJournal of Physical Chemistry B
Issue number14
StatePublished - Apr 13 2000

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry


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