Abstract
Protein recognition can be divided into two categories in terms of the interaction sites: (a) interactions that occur inside proteins, e.g. enzyme active sites; (b) interactions that occur on the surface of proteins. During the past two decades large numbers of synthetic molecules targeted to disrupt interior protein interactions have been shown to have medically important biological activities.1 However, artificially designed molecules that target the protein surface and disrupt its biological activity are rare.2 Considering the unique composition of charged, hydrophobic and hydrophilic domains on every protein’s surface, synthetic molecules that match the electrostatic features and topology of the protein targets might be expected to bind to the exterior and sterically prevent protein-ligand or protein-protein interactions. This in turn can provide a novel approach to modulating biological processes.
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Lin, Q., Park, H.S., Hamuro, Y., Hamilton, A.D. (1999). Protein Surface Recognition by Synthetic Receptors. In: Ungaro, R., Dalcanale, E. (eds) Supramolecular Science: Where It Is and Where It Is Going. NATO ASI Series, vol 527. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4554-1_11
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DOI: https://doi.org/10.1007/978-94-011-4554-1_11
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