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The principles of metal chelation provide significant opportunities for drug design that go beyond traditional notions of chelation as metal sequestration and elimination. Exploring these other possibilities could lead to pharmacological interventions that alter the concentration, distribution, or reactivity of metals in targeted ways for therapeutic benefit. A good example is fragment-based lead design (FBLD) that has been used to identify new metal-binding groups for metalloenzyme inhibitors. This and other approaches exploit the presence of the metal ion in these enzymes for the development of synthetic small molecules with therapeutic potential.

Natural products have contributed to the development of many drugs for diverse indications and they continue to be an important source of leads for new medicines, despite reduced interest from large pharmaceutical companies. The development of new technologies including fragment-based drug discovery (FBDD) has revolutionized the screening of natural products as potential therapeutic agents.

In the past decade, fragment based drug design (FBDD) has risen as a new and effective approach to identify lead compounds and continues to show great promise in drug discovery. It requires the use of sensitive techniques such as X-ray crystallography to identify hits among low molecular weight fragment compounds that have a weak binding affinity to a drug target. The hit fragments could be then structurally optimized to lead compounds with high affinity and specificity.

For the last several decades, progress in RNA investigations revealed earlier underestimated importance of RNA in normal and abnormal cellular processes. It is now clear that regulation of translation and transcription, protein and enzyme functions that have commonly been attributed to proteins are frequently in RNAs' competency.

The multitude of recent research articles devoted to the wide variety of diseases, including viral and bacterial infections, cancer and degenerative processes, emphasized the high potential of approaches targeted on the structure of particular RNA.

Majority of biological processes would not be possible without protein–protein interactions (PPIs). Human interactome is estimated to comprise more than 600,000 PPIs, and only a small part of them has been studied. PPIs are associated with a growing number of diseases and have garnered significant interest in pharmaceutical research offering attractive opportunities for therapeutic intervention. Designing molecules that interfere with the formation of protein complexes is one of the recent challenges in drug design.