title: Hydrogel lens monomer constituents modulate protein sorption.
abstract: OBJECTIVE
  To examine the effect of hydrogel lens monomer constituents on protein sorption.
  
  
  METHODS
  A series of hydroxyethylmethacrylate (HEMA)-based hydrogels with various amounts of methacrylic acid (MAA) or N-vinyl pyrrolidone (NVP) were synthesized. A radiolabel tracer technique was used to measure the amount of protein adsorbed on or penetrating into the hydrogels. Penetration of fluorescence-labeled proteins in the hydrogels was studied by laser scanning confocal microscopy. Single-protein solutions of human serum albumin (HSA) and hen egg lysozyme were studied.
  
  
  RESULTS
  Inclusion of the comonomers MAA or NVP in hydrogels resulted in an increase in water content and also had a strong impact on protein sorption. An increase in the amount of MAA in the poly(HEMA-co-MAA) hydrogels increased lysozyme adsorption and penetration but reduced HSA adsorption. However, the amount of protein adsorbed for both HSA and lysozyme increased with the amount of NVP in the poly(HEMA-co-NVP) hydrogels. In contrast to the marked effect of MAA on protein sorption, in particular, on lysozyme sorption, NVP had little influence on protein sorption. When a hydrogel contains both MAA and NVP, MAA has the dominant effect on protein sorption-in particular, on lysozyme sorption. Furthermore, a large difference was observed in the amount of lysozyme adsorbed on the hydrogels that had similar water contents but little variation in adsorption of HSA.
  
  
  CONCLUSIONS
  Negatively charged carboxyl groups of the MAA constituent may influence lysozyme sorption in two ways: by electrostatic attraction and by increasing the possibility for the small lysozyme molecule to penetrate the hydrogels. Interactions of the surface lactam groups of NVP with proteins may be attributable to the attraction of proteins to NVP. Water content is not a primary factor in determining protein adsorption. It appears that the monomer constituents, such as MAA or NVP, control protein adsorption.
authors.affiliation: Cooperative Research Centre for Eye Research and Technology, The University of New South Wales, Sydney, Australia. q.garrett@cclru.unsw.edu.au
authors.forename: Q
authors.initials: Q
authors.lastname: Garrett
authors.forename: B
authors.initials: B
authors.lastname: Laycock
authors.forename: R W
authors.initials: RW
authors.lastname: Garrett
mesh_terms: D000327:Adsorption; D003261:Contact Lenses; D008689:Methacrylates / Q000737:chemistry / Q000378:metabolism*; D018613:Microscopy, Confocal; D009113:Muramidase / Q000493:pharmacokinetics*; D011102:Polyhydroxyethyl Methacrylate / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011760:Pyrrolidinones / Q000737:chemistry / Q000378:metabolism*; D012709:Serum Albumin / Q000493:pharmacokinetics*; D055672:Static Electricity
chemical_list: D008689:Methacrylates; D011760:Pyrrolidinones; D012709:Serum Albumin; C008384:methacrylic acid; D011102:Polyhydroxyethyl Methacrylate; C042670:N-vinyl-2-pyrrolidinone; D009113:Muramidase