Targeting EphA2-Sam and Its Interactome: Design and Evaluation of Helical Peptides Enriched in Charged Residues(352 views visite) Mercurio FA, Marasco D, Di Natale C, Pirone L, Costantini S, Pedone EM, Leone M
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-4227linking), 2016 Nov 17; 17(22): 2179-2188.
Keywords Parole chiave: Epha2, Sam Domain, Cancer, Conformational Analysis, Drug Design, Helical Peptides,
Affiliations Affiliazioni: *** IBB - CNR ***
Institute of Biostructures and Bioimaging, National Research Council, Via Mezzocannone 16, 80134, Naples, Italy., Department of Pharmacy, University of Naples "Federico II", Via Mezzocannone 16, 80134, Naples, Italy., Department of Biology, University of Naples "Federico II", Via Cinthia 4, 80126, Naples, Italy., CROM, IRCCS-Istituto Nazionale Tumori "Fondazione G. Pascale", Via Mariano Semmola 52, 80131, Naples, Italy.,
References Riferimenti: Not available. Non disponibili.
Targeting EphA2-Sam and Its Interactome: Design and Evaluation of Helical Peptides Enriched in Charged Residues
The EphA2 receptor controls diverse physiological and pathological conditions and its levels are often upregulated in cancer. Targeting receptor overexpression, through modulation of endocytosis and consequent degradation, appears to be an appealing strategy for attacking tumor malignancy. In this scenario, the Sam domain of EphA2 plays a pivotal role because it is the site where protein regulators of endocytosis and stability are recruited by means of heterotypic Sam-Sam interactions. Because EphA2-Sam heterotypic complexes are largely based on electrostatic contacts, we have investigated the possibility of attacking these interactions with helical peptides enriched in charged residues. Several peptide sequences with high predicted helical propensities were designed, and detailed conformational analyses were conducted by diverse techniques including NMR, CD, and molecular dynamics (MD) simulations. Interaction studies were also performed by NMR, surface plasmon resonance (SPR), and microscale thermophoresis (MST) and led to the identification of two peptides capable of binding to the first Sam domain of Odin. These molecules represent early candidates for the generation of efficient Sam domain binders and antagonists of Sam-Sam interactions involving EphA2.
Targeting EphA2-Sam and Its Interactome: Design and Evaluation of Helical Peptides Enriched in Charged Residues
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568 Records (504 escludendo Abstract e Conferenze). Impact factor totale: 2160.614 (1929.961 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 2107.671 (1849.932 escludendo Abstract e Conferenze).
Last modified by Ultima modifica di Marilisa Leone on in data Sunday 12 July 2020, 13:14:46 352 views visite. Last view on Ultima visita in data Wednesday 03 March 2021, 18:22:40