FBDD is an alternative to traditional high-throughput screening (HTS) and virtual screening (VS) which screens 'Lipinski compliant' small molecules. In contrast, FBDD screens 'fragments', typically with a molecular weight (MW) under 260 Da. Although 'fragment' hits typically exhibit weaker binding affinities than small molecules, they often form polar interactions with the receptor and possess favourable lipophilicity, limiting entropically-driven binding. Thus, 'fragments' can be an advantageous starting point for drug design and techniques to optimize their potency and physicochemical properties include fragment growing and fragment linking. The latter is of particular interest as proper linking of two 'fragments' such that the linked molecule does not perturb the constituents' interactions can lead to significant potency gain. This is attributed to favourable entropic effects and known as 'super-additivity'. In practice, fragment linking is challenging and 'super-additivity' is rarely achieved, owing to incompatible linkers disrupting the fragments' binding poses. Thus, improvements in linker design are critical to unlock the full potential of FBDD.