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Abstract
Cell-penetrating peptides show promise as versatile tools for intracellular delivery of therapeutic agents. Various peptides have originated from natural proteins with antimicrobial activity. We investigated the mammalian cell-penetrating properties of a 16-residue peptide with the sequence GRCRGFRRRCFCTTHC from the C-terminus tail of the Medicago truncatula defensin MtDef4. We evaluated the peptide’s ability to penetrate multiple cell types. Our results demonstrate that the peptide efficiently penetrates mammalian cells within minutes and at a micromolar concentration. Moreover, upon N-terminal fusion to the fluorescent protein GFP, the peptide efficiently delivers GFP into the cells. Despite its remarkable cellular permeability, the peptide has only a minor effect on cellular viability, making it a promising candidate for developing a cell-penetrating peptide with potential therapeutic applications.
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Details
1 Tel Aviv University, Department of Oral Biology, Faculty of Medicine, The Goldschleger School of Dental Medicine, Tel Aviv, Israel (GRID:grid.12136.37) (ISNI:0000 0004 1937 0546)
2 Tel-Aviv University, BLAVATNIK CENTER for Drug Discovery, Tel Aviv, Israel (GRID:grid.12136.37) (ISNI:0000 0004 1937 0546)
3 The Hebrew University of Jerusalem, Institute of Biochemistry, Food Science and Nutrition, The Robert H. Smith Faculty of Agricultural, Food and Environment, Rehovot, Israel (GRID:grid.9619.7) (ISNI:0000 0004 1937 0538)