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• W2891867549 abstract "E2F1-3a overexpression due to amplification or to mutation or loss of the retinoblastoma gene, induces genes involved in DNA synthesis and leads to abnormal cellular proliferation, tumor growth, and invasion. Therefore, inhibiting the overexpression of one or more of these activating E2Fs is a recognized target in cancer therapeutics. In previous studies we identified by phage display, a novel 7-mer peptide (PEP) that bound tightly to an immobilized consensus E2F1 promoter sequence, and when conjugated to penetratin to increase its uptake into cells, was cytotoxic to several malignant cell lines and human prostate and small cell lung cancer xenografts. Based on molecular simulation studies that showed that the D-Arg penetratin peptide (D-Arg PEP) secondary structure is more stable than the L-Arg PEP, the L-Arg in the peptide was substituted with D-Arg. In vitro studies confirmed that it was more stable than the L- form and was more cytotoxic as compared to the L-Arg PEP when tested against the human castrate resistant cell line, DU145 and the human lung cancer H196 cell line. When encapsulated in PEGylated liposomes, the D-Arg-PEP potently inhibited growth of the DU145 xenograft in mice. Our findings validate D- Arg PEP, an inhibitor of E2F1and 3a transcription, as an improved second generation drug candidate for targeted molecular therapy of cancers with elevated levels of activated E2F(s)." @default.
• W2891867549 created "2018-09-27" @default.
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• W2891867549 date "2018-09-07" @default.
• W2891867549 modified "2023-09-27" @default.
• W2891867549 title "Modeling and antitumor studies of a modified L-penetratin peptide targeting E2F in lung cancer and prostate cancer" @default.
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• W2891867549 doi "https://doi.org/10.18632/oncotarget.26064" @default.
• W2891867549 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6161789" @default.
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