The many weak interactions that might be involved in protein-protein and protein-ligand binding are well understood on a functional group-by-functional group basis. But the cooperation of many such �simple� interactions to drive binding always involves complex, non-additive effects that are difficult to predict and understand. This makes the dissection of the energetic contributions of individual functional groups to an overall complexation event a process that is fraught with difficulty. We will report here data arising from model recognition systems, protein structural surveys, and a series of structure/function relationships within a new family of antagonists of epigenetic reader protein interactions. Areas of discussion will include efforts to quantify the magnitude of the dipolar interactions of fluorine, the role of cation-pi interactions in protein-ligand recognition, and attempts to understand the roles of protein hydration and hydrophobicity in the recognition processes of epigenetic reader proteins.

Complex interplay of electrostatics and hydration effects in protein-ligand binding: Studying fluorine dipolar interactions and cation-pi interactions using model systems and new families of ligands for epigenetic protein motifs

245th National Meeting (2013)

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