Measurement of porcine haptoglobin in meat juice using surface acoustic wave biosensor technology.

Aim of the study was the application of biosensor technique to measure the concentration of an acute phase protein (APP) within complex matrices from animal origin. For the first time, acute phase protein haptoglobin (Hp) was detected from unpurified meat juice of slaughter pigs by a label-free biosensor-system, the SAW-based sam®5 system. The system uses a sensor chip with specific antibodies to catch Hp while the mass-related phase shift is measured. The concentration is calculated as a function of these measured phase shifts. The results correlate very well with reference measurement results obtained by enzyme-linked immunosorbent assay (ELISA), R=0.98. The robust setup of the surface acoustic wave (SAW)-based system and its ability to measure within very short time periods qualifies it for large-scale analyses and is apt to identify rapidly pigs in the meat production process whose consumption would have an increased risk for consumers.

Surface acoustic wave biosensor as a tool to study the interaction of antimicrobial peptides with phospholipid and lipopolysaccharide model membranes.

Surface acoustic wave biosensors are a powerful tool for the study of biomolecular interactions. The modulation of a surface-confined acoustic wave is utilized here for the analysis of surface binding. Phase and amplitude of the wave correspond roughly to mass loading and viscoelastic properties of the surface, respectively. We established a procedure to reconstitute phospholipid and lipopolysaccharide bilayers on the surface of a modified gold sensor chip to study the mode of action of membrane-active peptides. The procedure included the formation of a self-assembled monolayer of 11-mercaptoundecanol, covalent coupling of carboxymethyl-dextran, and subsequent coating with a poly- l-lysine layer. The lipid coverage of the surface is highly reproducible and homogeneous as demonstrated in atomic force micrographs. Ethanol/triton treatment removed the lipids completely, which provided the basis for continuous sequences of independent experiments. The setup was applied to investigate the binding of human cathelicidin-derived peptide LL32, as an example for antimicrobial peptides, to immobilized phosphatidylserine membranes. The peptide-membrane interaction results in a positive phase shift and an increase in amplitude, indicating a mass increase along with a loss in viscosity. This suggests that the bilayer becomes more rigid upon interaction with LL32.