Optical tweezers to study single protein A/immunoglobulin G interactions at varying conditions.
Optical tweezers (OT) are ideally suited to study the interaction of single receptor-ligand bonds. Here we introduce a newly developed assay using OT to investigate the interactions between Protein A from Staphylococcus aureus and Immunoglobulin G from rabbit serum (RIgG). We demonstrate that the rupture forces depend on the loading rate and on the sodium chloride concentration. The measured loading rate effect is well known in the literature and the data we obtained were found to be in good agreement with an already published theoretical model. The dependence of the rupture forces on the salt concentration demonstrates the influence of hydrophobic interactions on the bond strength. Our experimental setup can probe the interaction between a single receptor and its specific ligand under changing conditions and hence offers manifold applications in single molecule biotechnology.
Salomo
Mathias
M
Institut für Experimentelle Physik I, Universität Leipzig, Linnèstrasse 5, 04103, Leipzig, Germany. msalomo@rz.uni-leipzig.de
Keyser
Ulrich F
UF
Struhalla
Marc
M
Kremer
Friedrich
F
D003198:Computer Simulation; D004548:Elasticity; D007074:Immunoglobulin G / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D052898:Optical Tweezers; D011485:Protein Binding; D013205:Staphylococcal Protein A / Q000737:chemistry*; D013314:Stress, Mechanical
D007074:Immunoglobulin G; D013205:Staphylococcal Protein A