Ellipsometry was used to study the effects of surface energetics
and temperature on the equilibrium adsorptive behavior exhibited by
β-lactoglobulin. β-Lactoglobulin isotherms at 25, 37, and 55°C were
constructed for this purpose. The surfaces of acrylic, polycarbonate,
polyester, glass, and #304 stainless steel were contacted with protein
solutions of varying...
Surface tension kinetics exhibited by selected stability mutants of T4 lysozyme at the air-water interface were monitored with DuNoüy tensiometry. Mutant lysozymes were produced by substitution of isoleucine at position 3 with cysteine, leucine, tryptophan and glycine. Each substitution resulted in an altered structural stability quantified by a change in...
The adsorption kinetics exhibited by selected charge mutants of T4 lysozyme at
silanized silica surfaces were monitored with in situ ellipsometry. Mutant lysozymes were
produced by substitution of lysine (Lys) with glutamic acid (Glu). Each substitution
resulted in a decrease in the net charge of the protein by 2 units....
The effect of pH and ionic strength on the equilibrium adsorptive
behavior of β-lactoglobulin onto hydrophobic and hydrophilic
silicon surfaces was studied using ellipsometry. Plots of amount
adsorbed (μg protein/cm²) as a function of protein concentration
(mg/ml) exhibited attainment of plateau values beyond a protein
concentration of 0.250 mg/ml. At...
Nisin, an amphiphilic, antimicrobial peptide, has been shown to integrate into the hydrophobic inner region of poly(ethylene oxide) (PEO) brush layers; however, the presence of integrated nisin may compromise the protein repulsive character of the PEO layer. In particular, the introduction of fibrinogen to nisin-loaded brush layers has been observed...