Monolayers of derivatized poly( l -lysine)-grafted poly(ethylene glycol) on metal oxides as a class of biomolecular interfaces | Zendy

Laurence Ruiz-Taylor | Zendy; T. Martin | Zendy; Frank Zaugg | Zendy; Krista Witte | Zendy; P. Indermuhle | Zendy; Steffen Nock | Zendy; Peter Wagner | Zendy

Open Access

Monolayers of derivatized poly( l -lysine)-grafted poly(ethylene glycol) on metal oxides as a class of biomolecular interfaces

Author(s) -

Laurence Ruiz-Taylor,

T. Martin,

Frank Zaugg,

Krista Witte,

P. Indermuhle,

Steffen Nock,

Peter Wagner

Publication year - 2001

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.98.3.852

Subject(s) - streptavidin , ethylene glycol , biotinylation , monolayer , peg ratio , copolymer , chemistry , protein adsorption , biotin , adsorption , lysine , combinatorial chemistry , polymer chemistry , materials science , organic chemistry , polymer , biochemistry , amino acid , finance , economics

We report on the design and characterization of a class of biomolecular interfaces based on derivatized poly(l-lysine)-grafted poly(ethylene glycol) copolymers adsorbed on negatively charged surfaces. As a model system, we synthesized biotin-derivatized poly(l-lysine)-grafted poly(ethylene glycol) copolymers, PLL-g-[(PEGm)((1-x)) (PEG-biotin)(x)], where x varies from 0 to 1. Monolayers were produced on titanium dioxide substrates and characterized by x-ray photoelectron spectroscopy. The specific biorecognition properties of these biotinylated surfaces were investigated with the use of radiolabeled streptavidin alone and within complex protein mixtures. The PLL-g-PEG-biotin monolayers specifically capture streptavidin, even from a complex protein mixture, while still preventing nonspecific adsorption of other proteins. This streptavidin layer can subsequently capture biotinylated proteins. Finally, with the use of microfluidic networks and protein arraying, we demonstrate the potential of this class of biomolecular interfaces for applications based on protein patterning.

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