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Int. J. Mol. Sci. 2015, 16(4), 7394-7412; doi:10.3390/ijms16047394

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
Permanent address: Center for Advanced Biomaterials for Health Care@CRIB, Istituto Italiano di Tecnologia, 80125 Naples, Italy.
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Author to whom correspondence should be addressed.
Academic Editor: Vladimir N. Uversky
Received: 17 January 2015 / Revised: 1 March 2015 / Accepted: 6 March 2015 / Published: 2 April 2015
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Abstract

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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

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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