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Identification of Inhibitors of Biological Interactions Involving Intrinsically Disordered Proteins

Department of Pharmacy, Centro Interuniversitario di Ricerca sui Peptidi Bioattivi (CIRPEB), University of Naples "Federico II", DFM-Scarl, 80134 Naples, Italy
Author to whom correspondence should be addressed.
Permanent address: Center for Advanced Biomaterials for Health [email protected], Istituto Italiano di Tecnologia, 80125 Naples, Italy.
Academic Editor: Vladimir N. Uversky
Int. J. Mol. Sci. 2015, 16(4), 7394-7412;
Received: 17 January 2015 / Revised: 1 March 2015 / Accepted: 6 March 2015 / Published: 2 April 2015
Protein–protein interactions involving disordered partners have unique features and represent prominent targets in drug discovery processes. Intrinsically Disordered Proteins (IDPs) are involved in cellular regulation, signaling and control: they bind to multiple partners and these high-specificity/low-affinity interactions play crucial roles in many human diseases. Disordered regions, terminal tails and flexible linkers are particularly abundant in DNA-binding proteins and play crucial roles in the affinity and specificity of DNA recognizing processes. Protein complexes involving IDPs are short-lived and typically involve short amino acid stretches bearing few “hot spots”, thus the identification of molecules able to modulate them can produce important lead compounds: in this scenario peptides and/or peptidomimetics, deriving from structure-based, combinatorial or protein dissection approaches, can play a key role as hit compounds. Here, we propose a panoramic review of the structural features of IDPs and how they regulate molecular recognition mechanisms focusing attention on recently reported drug-design strategies in the field of IDPs. View Full-Text
Keywords: flexible protein regions; peptides; human diseases flexible protein regions; peptides; human diseases
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Marasco, D.; Scognamiglio, P.L. Identification of Inhibitors of Biological Interactions Involving Intrinsically Disordered Proteins. Int. J. Mol. Sci. 2015, 16, 7394-7412.

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