MBIANDA, Johanne; BAKAIL, May; ANDRE, Christophe; MOAL, Gwenaelle; PERRIN, Marie E.; PINNA, Guillaume; GUEROIS, Raphael; BECHER, Francois; LEGRAND, Pierre; TRAORE, Seydou; DOUAT, Celine; GUICHARD, Gilles; OCHSENBEIN, Francoise

doi:10.1126/sciadv.abd9153

MBIANDA, Johanne
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

BAKAIL, May

ANDRE, Christophe
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

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Science Advances. 2021, vol. 7, n° 12

Resumen en inglés

Sequence-specific oligomers with predictable folding patterns, i.e., foldamers, provide new opportunities to mimic.-helical peptides and design inhibitors of protein-protein interactions. One major hurdle of this strategy is to retain the correct orientation of key side chains involved in protein surface recognition. Here, we show that the structural plasticity of a foldamer backbone may notably contribute to the required spatial adjustment for optimal interaction with the protein surface. By using oligoureas as. helix mimics, we designed a foldamer/peptide hybrid inhibitor of histone chaperone ASF1, a key regulator of chromatin dynamics. The crystal structure of its complex with ASF1 reveals a notable plasticity of the urea backbone, which adapts to the ASF1 surface to maintain the same binding interface. One additional benefit of generating ASF1 ligands with nonpeptide oligourea segments is the resistance to proteolysis in human plasma, which was highly improved compared to the cognate alpha-helical peptide.< Leer menos

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https://oskar-bordeaux.fr/handle/20.500.12278/106509

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http://dx.doi.org/10.1126/sciadv.abd9153

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https://en.bio-protocol.org/cjrap.aspx?eid=10.1126/sciadv.abd9153

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CBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248

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Optimal anchoring of a foldamer inhibitor of ASF1 histone chaperone through backbone plasticity

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DOI

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Centros de investigación