A virus has a very intricate structure. On surface area of all viruses, there are tiny knits of some proteins. And these are mainly responsible for the serious effect, created by virus after having an interaction with our cells or the favorable environment in the surrounding area. If there is any alteration in the series of protein, then the surface turns out to be hydrophobic. It means that the part may repel water, and as a result, a sticky substance is formed on the surface.
One of the members (Heldt) at chemical research department of Michigan University has stated something about the new innovations of the researchers. At present, many of the associates of this University are trying to have a concept on how the hydrophobicity on virus surface is to be applied for the improvement in the production of vaccines.
A comparison on a variety of results-
Heldt has also claimed that dealing with purification of vaccine means working on the interactions on surface. While there is a disintegration of all components, they may not be applied as a kind of remedy. In addition to it, identification and removal of viruses also have a direct relation with all these interactions. Such facts may be very useful to the experts to know the interactions of virus or germs with our cells. The good news is that Caryn Heldt as well as her associates has made a comparison of different computational and experimental techniques in order to know the chemistry of surface.
Hydrophobicity- How the researchers tried to identify it-
Hydrophobicity may be defined as a property, which is found in a molecule that seems to be repelled or resisted from water mass. As the hydrophobicity of virus is quite tough to determine, the associates of Heldt emphasize the use of hydrophobicity pattern. These experts have also evaluated the possible measurements of hydrophobicity on the basis of protein, present in virus. They have tested out the specimens with the application of two chromatography types. One is the blend of chemicals and another one is fluorescent tints, which cause the appearance of hydrophobic, gluey spots on surface of proteins. The main fact is that all measurements try to make out something, which is easily accessible.
According to Heldt, the capsid of virus is so big that it is intricate to do measurements. To clarify the issues, Heldt has explained that capsid refers to outer shell, which comprises sixty same types of proteins, such as, VP1, 2 or 3. Heldt along with other researchers has tested VP2 and its exposed areas. There is a good link among all the results. And it reveals that any virus, including PPV has hydrophobicity, which is easily assessable. After having a better understanding of these measurements, the researchers may be able to detect virus.