Abstract
Overexpression of RAD51 protein was found to increase drug resistance in breast cancer cells. Breast cancer susceptibility gene 1 (BRCA1) protein can specifically bind to RAD51 protein and regulate the expression level of RAD51 protein. Based on previous studies, eight modified peptides were obtained by modifying the N-terminus of the key peptide segment 856–871 of BRCA1 with nicotinic acid (NA) and its derivatives. The interaction of BRCA1856-871 and modified peptides with the RAD51158-180 target peptide was investigated by fluorescence and circular dichroism spectroscopies. The results showed that the binding ability of 2-TFM-NA-PP to RAD51158-180 was significantly enhanced. BRCA1856-871 and modified peptides were studied by in vitro cell experiments. The results showed that the antitumor activity of 5-TFM-NA-PP was significantly enhanced compared with BRCA1856-871.
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