Figure 1. General configuration of biosensors. The biological recognizing element
(enzyme, antibody, receptor, DNA, cell, etc.) is in intimate contact with a physical transducer that converts the biorecognition process into a measurable signal (electrical, optical, etc). Catalytic biosensors have enzyme as biorecognition element and affinity biosensors are based on antibodies, DNA, cells or other type of receptor.
intimate contact with a physical transducer that converts the biorecogni-
tion process into a measurable signal (electrical, optical, and so on) as seen in Figure 1. Biosensors are commonly classified as immunosensors, enzy- matic (catalytic), non-enzymatic receptor, whole-cell (microbial sensors) or nucleic acid (DNA) biosensors, according to the biological recognition element. Immunosensors are affinity-based sensors designed to detect the direct binding of an antibody (Ab) to an antigen (Ag) to form an immunocom- plex at the transducer surface. Depending on the transducer technology employed, immunosensors can be divided into three principal classes: opti- cal, electrochemical and piezoelectrical. They are based on the principles of solid-phase immunoassays, where the immuno-reagent (Ab or Ag) is immo- bilized on a solid support, so that the interaction takes place at the solid- liquid interface. Antibodies are globular proteins produced by the immune system of mammals as a defense against foreign agents (antigen, Ag). The struc- ture of the antibody molecules is usually typified by the immunoglobulin G (IgG) subclass, which is the most commonly used in immunochemical application. The IgGs (molecular weight of 150 kDa) are composed of four polypeptide chains: two identical heavy (H) and two identical light (L) chains (50 kDa and 23 to 25 kDa, respectively) interlinked by disulphide bridges (see Figure 2).40 The region that carries the antigen binding sites is known as the Fab fragment, and the constant (crystallized) region that is involved in immune regulation is termed Fc. Both H and L chains are