RGD-grafted poly-L-lysine-graft-(polyethylene glycol) copolymers block non-specific protein adsorption while promoting cell adhesion

Biotechnol Bioeng. 2003 Jun 30;82(7):784-90. doi: 10.1002/bit.10625.

Abstract

A novel class of surface-active copolymers is described, designed to protect surfaces from nonspecific protein adsorption while still inducing specific cell attachment and spreading. A graft copolymer was synthesized, containing poly-(L-lysine) (PLL) as the backbone and substrate binding and poly(ethylene glycol) (PEG) as protein adsorption-resistant pendant side chains. A fraction of the grafted PEG was pendantly functionalized by covalent conjugation to the peptide motif RGD to induce cell binding. The graft copolymer spontaneously adsorbs from dilute aqueous solution onto negatively charged surfaces. The performance of RGD-modified PLL-g-PEG copolymers was analyzed in protein adsorption and cell culture assays. These coatings efficiently blocked the adsorption of serum proteins to Nb(2)O(5) and tissue culture polystyrene while specifically supporting attachment and spreading of human dermal fibroblasts. This surface functionalization technology is expected to be valuable in both the biomaterial and biosensor fields, because different signals can easily be combined, and sterilization and application are straightforward and cost-effective.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Blood Proteins / chemistry*
  • Cell Adhesion / physiology*
  • Cell Division / physiology
  • Coated Materials, Biocompatible / chemical synthesis
  • Coated Materials, Biocompatible / chemistry*
  • Drug Stability
  • Fibroblasts / cytology
  • Fibroblasts / physiology*
  • Humans
  • Oligopeptides / chemistry*
  • Polyethylene Glycols / chemistry*
  • Polylysine / chemistry*
  • Protein Binding
  • Skin / cytology
  • Skin Physiological Phenomena
  • Surface Properties

Substances

  • Blood Proteins
  • Coated Materials, Biocompatible
  • Oligopeptides
  • Polylysine
  • Polyethylene Glycols
  • arginyl-glycyl-aspartic acid