Grafted block complex coacervate core micelles and their effect on protein adsorption on silica and polystyrene

A.M. Brzozowska, A. de Keizer, W. Norde, C. Detrembleur, M.A. Cohen Stuart

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)

Abstract

We have studied the formation and the stability of grafted block complex coacervate core micelles (C3Ms) in solution and the influence of grafted block C3M coatings on the adsorption of the proteins ß-lactoglobulin, bovine serum albumin, and lysozyme. The C3Ms consist of a grafted block copolymer PAA21-b-PAPEO14 (poly(acrylic acid)-b-poly(acrylate methoxy poly(ethylene oxide)), with a negatively charged PAA block and a neutral PAPEO block and a positively charged homopolymer P2MVPI (poly(N-methyl 2-vinyl pyridinium iodide). In solution, these C3Ms partly disintegrate at salt concentrations between 50 and 100 mM NaCl. Adsorption of C3Ms and proteins has been studied with fixed-angle optical reflectometry, at salt concentrations ranging from 1 to 100 mM NaCl. In comparison with the adsorption of PAA21-b-PAPEO14 alone adsorption of C3Ms significantly increases the amount of PAA21-b-PAPEO14 on the surface. This results in a higher surface density of PEO chains. The stability of the C3M coatings and their influence on protein adsorption are determined by the composition and the stability of the C3Ms in solution. A C3M-PAPEO14/P2MVPI43 coating strongly suppresses the adsorption of all proteins on silica and polystyrene. The reduction of protein adsorption is the highest at 100 mM NaCl (>90%). The adsorbed C3M-PAPEO14/P2MVPI43 layer is partly removed from the surface upon exposure to an excess of ß-lactoglobulin solution, due to formation of soluble aggregates consisting of ß-lactoglobulin and P2MVPI43. In contrast, C3M-PAPEO14/P2MVPI228 which has a fivefold longer cationic block enhances adsorption of the negatively charged proteins on both surfaces at salt concentrations above 1 mM NaCl. A single PAA21-b-PAPEO14 layer causes only a moderate reduction of protein adsorption.
Original languageEnglish
Pages (from-to)1081-1095
JournalColloid and Polymer Science
Volume288
Issue number10-11
DOIs
Publication statusPublished - 2010

Keywords

  • bovine serum-albumin
  • beta-lactoglobulin
  • polymeric micelles
  • chain stiffness
  • surfaces
  • binding
  • dependence
  • monolayers
  • reduction
  • copolymer

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