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The relationship between contact lens surface charge and in-vitro protein deposition levels

Paper ID Volume ID Publish Year Pages File Format Full-Text
13785 903 2001 4 PDF Available
Title
The relationship between contact lens surface charge and in-vitro protein deposition levels
Abstract

The adsorption of lysozyme and human serum albumin (HSA) onto hydrogel contact lenses was investigated as a function of lens surface charge. Anionic, cationic and non-ionic contact lenses were deposited using single protein solutions of identical pH and osmolarity. Protein deposition was analyzed using matrix assisted laser desorption ionization mass spectrometry (MALDI-ToF MS) and compared to a direct UV protein analysis method, the bicinchoninic acid (BCA) assay. The results showed remarkable consistency between the two techniques.By inference of results from analyses of sample solutions, lysozyme, a positively charged protein at physiological pH, was only detected on the anionic surface charged contact lenses, presumably a result of electrostatic interactions. Neither the cationic nor the non-ionic lenses deposited lysozyme, possibly due to charge repulsion. HSA, a negatively charged protein at physiological pH, was detected on the cationic lenses, again as a result of electrostatic interactions. The fact that HSA was not observed on either the anionic or non-ionic charged species further demonstrates the effect of charge repulsion.

Keywords
Anionic; Cationic; Non-ionic; Lysozyme; Human serum albumin (HSA); Bicinchoninic acid (BCA) assay; Matrix assisted laser desorption ionization mass spectrometry (MALDI-ToF MS)
First Page Preview
The relationship between contact lens surface charge and in-vitro protein deposition levels
Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 22, Issue 24, 15 December 2001, Pages 3257–3260
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering