Highly protein-resistant coatings from well-defined diblock copolymers containing sulfobetaines

Langmuir. 2006 Feb 28;22(5):2222-6. doi: 10.1021/la052962v.

Abstract

Three well-defined diblock copolymers of poly(sulfobetaine methacrylate) [poly(SBMA)] and poly(propylene oxide) (PPO) were synthesized by the sequential addition of SBMA monomer to fixed amounts of PPO using an atom transfer radical polymerization method and varying poly(SBMA) lengths. These copolymers were characterized by 1H NMR and aqueous gel permeation chromatography. These copolymers were physically adsorbed onto a surface plasmon resonance (SPR) sensor surface covered by methyl-terminated self-assembled monolayers, followed by the in situ evaluation of protein adsorption on the adsorbed copolymers. It is found that the behavior of the protein adsorption depends on the molecular weight of the copolymers. Results show that the diblock copolymers containing poly(SBMA) can be highly protein resistant when surface SBMA densities are well controlled. Thus, copolymers containing zwitterionic groups are ideal for resisting protein adsorption when the surface density of zwitterionic groups is controlled.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adsorption
  • Animals
  • Betaine / analogs & derivatives*
  • Betaine / chemistry
  • Cattle
  • Coated Materials, Biocompatible / chemistry
  • Fibrinogen / chemistry
  • In Vitro Techniques
  • Magnetic Resonance Spectroscopy
  • Molecular Structure
  • Muramidase / chemistry
  • Polymers / chemistry*
  • Polymethacrylic Acids / chemistry
  • Propylene Glycols / chemistry
  • Proteins / chemistry*
  • Serum Albumin, Bovine / chemistry
  • Surface Plasmon Resonance

Substances

  • Coated Materials, Biocompatible
  • Polymers
  • Polymethacrylic Acids
  • Propylene Glycols
  • Proteins
  • polymethacrylic acid
  • polypropylene glycol
  • Serum Albumin, Bovine
  • Betaine
  • sulfobetaine
  • Fibrinogen
  • Muramidase