@article{MTMT:30609649,
	title = {Recognition of ASF1 by Using Hydrocarbon-Constrained Peptides.},
	url = {https://m2.mtmt.hu/api/publication/30609649},
	author = {Bakail, May and Rodriguez-Marin, Silvia and Hegedüs, Zsófia and Perrin, Marie E. and Ochsenbein, Francoise and Wilson, Andrew J.},
	doi = {10.1002/cbic.201800633},
	journal-iso = {CHEMBIOCHEM},
	journal = {CHEMBIOCHEM},
	volume = {20},
	unique-id = {30609649},
	issn = {1439-4227},
	abstract = {Inhibiting the histone H3-ASF1 (anti-silencing function 1) protein-protein interaction (PPI) represents a potential approach for treating numerous cancers. As an α-helix-mediated PPI, constraining the key histone H3 helix (residues 118-135) is a strategy through which chem. probes might be elaborated to test this hypothesis. In this work, variant H3118-135 peptides bearing pentenylglycine residues at the i and i+4 positions were constrained by olefin metathesis. Biophys. analyses revealed that promotion of a bioactive helical conformation depends on the position at which the constraint is introduced, but that the potency of binding towards ASF1 is unaffected by the constraint and instead that enthalpy-entropy compensation occurs. [on SciFinder(R)]},
	year = {2019},
	eissn = {1439-7633},
	pages = {891-895},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167}
}