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, Mp
Publication date
January 2018
DOI Publisher
American Chemical Society (ACS)Abstract
LR 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 [Pro n]-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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