Affinity interactions on a liposome surface detected by ultrasound velocimetry.
In this work, we performed targeted immobilization of immunoglobulins by means of bacterial S-layer proteins from Bacillus coagulans E38-66/V1 recrystallized on liposomes, which were exploited as immobilization matrix for antibody (Ab)-human IgG. The study of interaction of rabbit or swine anti-human IgG as antigens (Ag) was performed by means of measuring changes of ultrasound velocity. We showed that at a temperature of 25 degrees C, the increment of ultrasound velocity [u] linearly decreased following an increase of concentration of Ag. The decrease of [u] was presumably due to changes of hydration of the membrane due to the binding process. Approximately 10 times lower changes of [u] were observed at 45 degrees C for Ag-Ab interaction as well as for nonspecific interaction of Ag with liposomes covered by S-layer without Ab. No substantial differences in the behaviour of [u] were observed for interactions of human IgG with rabbit or swine anti-human IgG.
Krivanek
R
R
Department of Biophysics and Chemical Physics, Faculty of Mathematics and Physics, Comenius University, Mlynská dolina F1, 842 48 Bratislava, Slovak Republic.
Rybar
P
P
Küpcü
S
S
Sleytr
U B
UB
Hianik
T
T
D001426:Bacterial Proteins / Q000378:metabolism*; D003720:Densitometry; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D008081:Liposomes; D014465:Ultrasonics
D001426:Bacterial Proteins; D007074:Immunoglobulin G; D008081:Liposomes