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Conformational Propensity and Biological Studies of Proline Mutated LR Peptides Inhibiting Human Thymidylate Synthase and Ovarian Cancer Cell Growth
journal contribution
posted on 2018-07-23, 00:00 authored by Puneet Saxena, Leda Severi, Matteo Santucci, Laura Taddia, Stefania Ferrari, Rosaria Luciani, Gaetano Marverti, Chiara Marraccini, Donatella Tondi, Marco Mor, Laura Scalvini, Simone Vitiello, Lorena Losi, Sergio Fonda, Salvatore Pacifico, Remo Guerrini, Domenico D’Arca, Glauco Ponterini, Maria Paola CostiLR and [d-Gln4]LR peptides bind the monomer–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.
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Molecular dynamics calculationsintracellular protein modulationthymidylate synthaseProline Mutated LR Peptides Inhibiting Human Thymidylate SynthaseConformational Propensityproline-mutated LR peptidesOvarian Cancer Cell Growth LRcancer cell growthdichroism spectraBiological Studiescell growth inhibition
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