25.02.2013 Views

Nanotechnology-Enabled Sensors

Nanotechnology-Enabled Sensors

Nanotechnology-Enabled Sensors

SHOW MORE
SHOW LESS

You also want an ePaper? Increase the reach of your titles

YUMPU automatically turns print PDFs into web optimized ePapers that Google loves.

7.4.4 Using Proteins as Nanodevices<br />

7.4 Proteins in <strong>Nanotechnology</strong> <strong>Enabled</strong> <strong>Sensors</strong> 411<br />

In this section we will present a selection of protein-based components<br />

for the development of nanodevices as well as nanomaterials which can be<br />

useful in sensor technology.<br />

The conformations of proteins give them their unique functions based<br />

on their chemical properties. Proteins units can be engineered for conducting<br />

specific chemical reactions. The chemical and physical properties of a<br />

protein give it the ability to perform extraordinary dynamic processes.<br />

The biological properties of a protein depend on how it interacts physically<br />

and chemically with other molecules. For instance, antibodies attach<br />

to certain viruses or bacteria, enzymes can interact with substrates and<br />

molecules such as ATP (which will be explained later in this chapter) to<br />

catalyze reactions in proteins. Actin molecules attach to each other to form<br />

an actin filament which are extremely abundant in eukaryotic cells where it<br />

forms one of the major filaments of the cytoskeleton which gives shape to<br />

a cell. 92<br />

The binding of proteins to other chemicals is not always strong; in many<br />

cases it is actually weak. However, the binding always shows specificity,<br />

which means that each protein can only bind to one or at most a few molecules<br />

that it encounters. Such a nature can be efficiently used for making<br />

sentitive surfaces. The substance which is bound by a protein is called a<br />

ligand for that protein. This ligand can be an ion, a small molecule or a<br />

macromolecule. Ligand-protein binding is of great importance in sensor<br />

technology.<br />

Noncovalent bonds such as hydrogen bonds, ionic bonds, and the Van<br />

der Waals attractions as well as hydrophobic interactions are responsible<br />

for the ability of selective bind of a protein to a ligand. The effect of each<br />

bond can be weak but the simultaneous formation of many weak bonds between<br />

the protein and the ligand form the selective binding. Even the<br />

matching of the surface contour of the protein and ligand can be the reason<br />

for selective binding (Fig. 7.35), as molecules of the wrong shape cannot<br />

approach the active sites closely enough to bind, if indeed they could. The<br />

region of a protein that associates with a ligand is called a binding site.<br />

These sites usually consist of a cavity in the protein surface which is<br />

formed by the folding arrangement of the polypeptide chains.

Hooray! Your file is uploaded and ready to be published.

Saved successfully!

Ooh no, something went wrong!