MIT Logo Often drugs made out of antibodies are believed to be developed by keeping in mind certain factors like their effectiveness, their target zone, etc. On the other hand factors which follow later on may not have been taken into serious consideration. Under different circumstances, these drugs are believed to clump or get aggravated, among other things.

However, a new computer model is now believed to have been developed, which boasts of putting an end to this problem. This model called Spatial Aggregation Propensity (SAP) is presumed to aid designers in detecting the parts of the antibodies which may be more prone to attract other molecules. This detection may in turn lead to the modification of the antibodies in such a way so as to prevent such a clumping. This innovative development was made by the experts from the Massachusetts Institute of Technology (MIT).

Apparently, drugs made out of antibodies are presumed to have a short shelf life because of their tendency to clump together. Such a clumping together is further noted to affect their effectiveness.

Antibodies notably may even have the ability of treating grave diseases like cancer, arthritis and various other chronic inflammatory and infectious diseases. More so, patients themselves may also administer these drugs to themselves. However in such cases high doses may need to be administered, which may in turn require these drugs to be stored in high amounts. But this could render these drugs ineffective, due to their clumping together.

Lead investigator, Bernhardt Trout, Professor of Chemical Engineering, says that, “Drugs are usually developed with the criteria of how effective they’ll be, and how well they’ll bind to whatever target they’re supposed to bind. The problem is there are all of these issues down the line that were never taken into account.”

In order to overcome this commonly faced criterion, the MIT team along with Bernhard Helk from Novartis, were noted to have designed the SAP. They have stated that usually maximum aggregation noticed in antibodies may be taking place due to the interaction between specific parts of the proteins. This interaction is presumed to take place between the hydrophobic (water-fearing) sections of the proteins.

This latest model boasts of overcoming this problem. While the molecule is in solution, SAP is believed to be capable of witnessing the hydrophobic regions, and may even determine how much of those regions have been exposed. Apart from this, the model is also hypothetically capable of zeroing-in on specific sections which may be attributed for the aggregation, in contrast to just pointing out single sites.

After the detection of the hydrophobic regions, the experts may then be able to lower the amount of hydrophobicity of these regions and also make them stable by mutating the amino acids present there.

This newly developed model is believed to be of great help in solving the problem which may most often be faced by the drug companies trying to develop potential drugs out of antibodies.

These findings have been presented online in Proceedings of the National Academy of Sciences.