Conformational Propensity and Biological Studies of Proline Mutated LR Peptides Inhibiting Human Thymidylate Synthase and Ovarian Cancer Cell Growth

Published on 2018-08-10T14:04:49Z (GMT) by
<b>LR</b> and <b>[d-Gln</b><sup><b>4</b></sup><b>]­LR</b> 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 [Pro<sup><i>n</i></sup>]-peptides. <b>[Pro</b><sup><b>3</b></sup><b>]­LR</b> and <b>[Pro</b><sup><b>4</b></sup><b>]­LR</b> show improved cell growth inhibition and similar intracellular protein modulation compared with <b>LR</b>. These represent a step forward to the identification of more rigid and metabolically stable peptides.

Cite this collection

Saxena, Puneet; Severi, Leda; Santucci, Matteo; Taddia, Laura; Ferrari, Stefania; Luciani, Rosaria; et al. (2018): Conformational Propensity and Biological Studies of

Proline Mutated LR Peptides Inhibiting Human Thymidylate Synthase

and Ovarian Cancer Cell Growth. ACS Publications. Collection.