Biochemistry Questions / Discuss the importance of different drug structures, such as rings, charged groups, hydrophobic residues, and H-bond forming groups, in interacting with target proteins. How do these interactions contribute to drug binding?

Having the correct functional groups in the optimal location is necessary for a drug molecule to interact with the target protein successfully. Ring structures are able to donate and accept charge, charged groups can interact with oppositely charged groups on the target protein, hydrophobic residues allow interaction with hydrophobic residues on the target, and H-bond forming groups can produce hydrogen bonds to allow the drug to bind.

These different interactions are important in ensuring a drug is able to bind successfully to its target. Using combinations of these groups improves the selectivity of the drug molecule, reducing the likelihood of off target effects.

These groups are described in ‘Lipinski’s rule of 5’, which gives guidance on small molecule drugs and the factors they normally have.