April 2014
Volume 55, Issue 13
Free
ARVO Annual Meeting Abstract  |   April 2014
The effect of lactoferrin on lysozyme deposition and activity on silicone hydrogel contact lenses
Author Affiliations & Notes
  • Brad Hall
    CCLR School of Optometry and Vision Science, University of Waterloo, Waterloo, ON, Canada
  • Lyndon William Jones
    CCLR School of Optometry and Vision Science, University of Waterloo, Waterloo, ON, Canada
    Physics & Astronomy, University of Waterloo, Waterloo, ON, Canada
  • James Forrest
    CCLR School of Optometry and Vision Science, University of Waterloo, Waterloo, ON, Canada
    Physics & Astronomy, University of Waterloo, Waterloo, ON, Canada
  • Footnotes
    Commercial Relationships Brad Hall, None; Lyndon Jones, Alcon (F), Allergan (F), AMO (F), CooperVision (F), Essilor (F), Johnson & Johnson (F), TearScience (F), Visioneering (F); James Forrest, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science April 2014, Vol.55, 6061. doi:
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    • Get Citation

      Brad Hall, Lyndon William Jones, James Forrest; The effect of lactoferrin on lysozyme deposition and activity on silicone hydrogel contact lenses. Invest. Ophthalmol. Vis. Sci. 2014;55(13):6061.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: To determine the effect of lactoferrin on lysozyme deposition and activity on silicone hydrogel contact lenses.

Methods: Three commercially available silicone hydrogel contact lens materials (senofilcon A, lotrafilcon B, balafilcon A) were examined during the first 2 hours of interaction with lactoferrin and lysozyme. Total protein deposition was determined by I125 radiolabeling of lysozyme and lactoferrin. Based upon the masses and dimensions of each protein as well as the surface area of each contact lens, approximations of the composition of the layers of protein deposits were determined. The activity of lysozyme was determined by a recently developed micrococcal activity assay with extra steps to distinguish between activity on the surface and activity in solution.

Results: Lotrafilcon B showed up to a 50% reduction in protein deposition due to competitive adsorption for lactoferrin at all time points and lysozyme after 7.5 minutes. Senofilcon A and balafilcon A did not show any relevant competitive adsorption between lysozyme and lactoferrin. After 2 hours the mass of lactoferrin on senofilcon A and lotrafilcon B lenses was ~3x higher than the mass of lysozyme while for balafilcon A lenses the mass of lysozyme was ~4x higher than the mass of lactoferrin. After 2 hours, the protein composition of the outer surface layer of deposits (lysozyme:lactoferrin by mass) was: senofilcon A (1:1.7), lotrafilcon B (1:2), and balafilcon A (5.3:1). Co-adsorption of lactoferrin and lysozyme decreased the activity of desorbed lysozyme in solution for senofilcon A and lotrafilcon B, but co-adsorption had no effect on the activity of surface-bound lysozyme for all lens types investigated.

Conclusions: This study determined the effect of competitive adsorption on lactoferrin and lysozyme deposition and lysozyme activity. Competitive adsorption is material specific and the only relevant effect occurred with lotrafilcon B lenses. Co-adsorption of lysozyme and lactoferrin does not affect the activity of surface-bound lysozyme but can reduce the activity of subsequently desorbed lysozyme.

Keywords: 477 contact lens • 659 protein structure/function • 486 cornea: tears/tear film/dry eye  
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