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The Influence of Net Charge and Charge Location on Adsorption and Dodecyltrimethylammonium Bromide-Mediated Elutability of Bacteriophage T4 Lysozyme at Silica Surfaces

McGuire, J; Wahlgren, M LU and Arnebrant, T (1995) In Journal of Colloid and Interface Science 170(1). p.193-202
Abstract (Swedish)
The effect of net charge and charge location on the adsorption and dodecyltrimethylammonium bromide (DTAB)-mediated elutability of bacteriophage T4 lysozyme was monitored at hydrophilic and hydrophobic silica surfaces with in situ ellipsometry. Mutant lysozymes were produced by substitution of selected lysine residues with glutamic acid, each substitution thus decreasing the net charge of the protein by 2 units. The wild-type protein (net charge +9) and four mutant proteins, each of net charge +7 or +5, were purified from Escherichia coli strains harboring the desired expression vectors. Differences in interfacial behavior among the proteins were observed with respect to both the adsorption kinetics and the DTAB-mediated elutability... (More)
The effect of net charge and charge location on the adsorption and dodecyltrimethylammonium bromide (DTAB)-mediated elutability of bacteriophage T4 lysozyme was monitored at hydrophilic and hydrophobic silica surfaces with in situ ellipsometry. Mutant lysozymes were produced by substitution of selected lysine residues with glutamic acid, each substitution thus decreasing the net charge of the protein by 2 units. The wild-type protein (net charge +9) and four mutant proteins, each of net charge +7 or +5, were purified from Escherichia coli strains harboring the desired expression vectors. Differences in interfacial behavior among the proteins were observed with respect to both the adsorption kinetics and the DTAB-mediated elutability exhibited by each. No simple relationship between protein net charge and surface behavior was observed, indicating that the location of the charge replacements had the major effect on surface behavior. At hydrophilic surfaces, mutations allowing the most mobile regions of positive charge to more readily orient toward the interface increased that protein's resistance to elutability; at hydrophobic surfaces, mutations favoring or otherwise not inhibiting hydrophobic association between the protein and the surface increased the resistance to elutability. This was not related to protein net charge, but to the probable influence of the location of each substitution relative to the other mobile, solvent-exposed, charged side chains of the molecule. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Colloid and Interface Science
volume
170
issue
1
pages
10 pages
publisher
Elsevier
external identifiers
  • scopus:0029267481
ISSN
1095-7103
DOI
10.1006/jcis.1995.1088
language
English
LU publication?
yes
id
e02a58f5-f7ea-41ed-b088-622b3b3fde92
date added to LUP
2016-04-15 19:37:25
date last changed
2017-11-09 16:05:12
@article{e02a58f5-f7ea-41ed-b088-622b3b3fde92,
  abstract     = {The effect of net charge and charge location on the adsorption and dodecyltrimethylammonium bromide (DTAB)-mediated elutability of bacteriophage T4 lysozyme was monitored at hydrophilic and hydrophobic silica surfaces with in situ ellipsometry. Mutant lysozymes were produced by substitution of selected lysine residues with glutamic acid, each substitution thus decreasing the net charge of the protein by 2 units. The wild-type protein (net charge +9) and four mutant proteins, each of net charge +7 or +5, were purified from Escherichia coli strains harboring the desired expression vectors. Differences in interfacial behavior among the proteins were observed with respect to both the adsorption kinetics and the DTAB-mediated elutability exhibited by each. No simple relationship between protein net charge and surface behavior was observed, indicating that the location of the charge replacements had the major effect on surface behavior. At hydrophilic surfaces, mutations allowing the most mobile regions of positive charge to more readily orient toward the interface increased that protein's resistance to elutability; at hydrophobic surfaces, mutations favoring or otherwise not inhibiting hydrophobic association between the protein and the surface increased the resistance to elutability. This was not related to protein net charge, but to the probable influence of the location of each substitution relative to the other mobile, solvent-exposed, charged side chains of the molecule.},
  author       = {McGuire, J and Wahlgren, M and Arnebrant, T},
  issn         = {1095-7103},
  language     = {eng},
  number       = {1},
  pages        = {193--202},
  publisher    = {Elsevier},
  series       = {Journal of Colloid and Interface Science},
  title        = {The Influence of Net Charge and Charge Location on Adsorption and Dodecyltrimethylammonium Bromide-Mediated Elutability of Bacteriophage T4 Lysozyme at Silica Surfaces},
  url          = {http://dx.doi.org/10.1006/jcis.1995.1088},
  volume       = {170},
  year         = {1995},
}