Predicting undesirable drug interactions with promiscuous proteins in silico

Although computational tools have been used to predict tosic responses resulting from molecules binding either as substrates or inhibitors to proteins, there are complications to be resolved. Some proteins appear promiscuous in their ability to bind a diverse array of hydrophobic molecule. This promiscuity arises from the binding site simultaneously accomodating more than one molecule, multiple seperate binding sites, protein flexibility, or a combination of all these properties. With the availability, or more crystal structures for these non-target proteins, we should be able to predict binding in silico with a greater accuracy, thus avoiding or managing toxic side effects, therefore ultimately improving the success of drug discovery.