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- W2897419022 abstract "SISLL–TAT and TAT–SISLL were synthesized by modifying the N– or C–termini of cell-penetrating peptides as transacting activator of transcription TAT (47–57) by attaching BRCA1 (782–786) (SISLL). The novel peptides were synthesized through Fmoc solid-phase synthesis procedures and characterized by LCQ Fleet MS, 1H NMR and 13C NMR. SISLL–TAT and TAT–SISLL displayed forceful antibacterial activities against Staphylococcus aureus, Bacillus subtilis, Escherichia coli, and Salmonella typhimurium with low hemolysis. SISLL–TAT showed better antibacterial activity than TAT–SISLL, with the minimum inhibitory concentration (MIC) values of 10–33 μg·mL−1. The results of the DNA-binding activities showed that both SISLL-TAT and TAT-SISLL could interact with DNA via the minor groove mode, and the binding constants were 4.97 × 105 L·mol−1 and 4.42 × 105 L·mol−1 at 310 K, respectively. Circular dichroism analysis showed slight transformation of the lysozyme secondary structure caused by SISLL–TAT and TAT–SISLL. We also found that the novel peptides SISLL–TAT and TAT–SISLL targeted bacterial DNA resulting in cell death. This explains the antibacterial mechanism of SISLL–TAT and TAT–SISLL, and is a solid theoretical basis for further designing novel and highly effective antibiotics for clinical application." @default.
- W2897419022 created "2018-10-26" @default.
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- W2897419022 date "2019-02-01" @default.
- W2897419022 modified "2023-10-12" @default.
- W2897419022 title "DNA/Lysozyme-binding affinity study of novel peptides from TAT (47–57) and BRCA1 (782–786) in vitro by spectroscopic analysis" @default.
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- W2897419022 doi "https://doi.org/10.1016/j.saa.2018.10.041" @default.
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