Conformational Propensity and Biological Studies of Proline Mutated LR Peptides Inhibiting Human Thymidylate Synthase and Ovarian Cancer Cell Growth
Articolo
Data di Pubblicazione:
2018
Citazione:
Conformational Propensity and Biological Studies of Proline Mutated LR Peptides Inhibiting Human Thymidylate Synthase and Ovarian Cancer Cell Growth / Saxena, P., Severi, L., Santucci, M., Taddia, L., Ferrari, S., Luciani, R., Marverti, G., Marraccini, C., Tondi, D., Mor, M., Scalvini, L., Vitiello, S., Losi, L., Fonda, S., Pacifico, S., Guerrini, R., D’Arca, D., Ponterini, G., Costi, M.P.. - In: JOURNAL OF MEDICINAL CHEMISTRY. - ISSN 0022-2623. - 61:16(2018), pp. 7374-7380. [10.1021/acs.jmedchem.7b01699]
Abstract:
LR and [D-Gln4]LR peptides bind the mono- mer−monomer interface of human thymidylate synthase and inhibit cancer cell growth. Here, proline-mutated LR peptides were synthesized. Molecular dynamics calculations and circular dichroism spectra have provided a consistent picture of the conformational propensities of the [Pron]-peptides. [Pro3]LR and [Pro4]LR show improved cell growth inhibition and similar intracellular protein modulation compared with LR. These represent a step forward to the identification of more rigid and metabolically stable peptides.
Tipologia CRIS:
Articolo su rivista
Elenco autori:
Saxena, Puneet; Severi, Leda; Santucci, Matteo; Taddia, Laura; Ferrari, Stefania; Luciani, Rosaria; Marverti, Gaetano; Marraccini, Chiara; Tondi, Donatella; Mor, Marco; Scalvini, Laura; Vitiello, Simone; Losi, Lorena; Fonda, Sergio; Pacifico, Salvatore; Guerrini, Remo; D’Arca, Domenico; Ponterini, Glauco; Costi, Maria Paola
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