IMAGE: This is a cyclic decapeptide, which mimics the dimerization arm of the EGF receptor (EGFR), was previously found to be captured into cells. The authors have found the promising potential… view more
Credit: Department of Medicinal Chemistry,TMDU
Tokyo Medical and Dental University (TMDU) study identifies promising lead compound for delivery of therapeutically effective peptides
Tokyo – In the field of anticancer therapeutics, cationic antimicrobial peptides (AMPs) have gained prominence because of their cytotoxic and anticancer activity in drug-resistant cancer cells. Peptides are compounds consisting of two or more amino acids linked in a chain.
A membrane impermeable proapoptotic domain (PAD) peptide [KLAKLAK]2 is known to be an antimicrobial agent and to cause mitochondrial membrane disruption, followed by cell death. Most AMPs including PAD have antitumor functions because of a multifunctional host defense system of multicellular organisms; however, they cannot penetrate cell membranes, and alone, they have little cytotoxicity.
Previous studies have shown PAD peptides entering cells by their conjugation with cell-penetrating peptides (CPPs). Particularly, a team of Tokyo Medical and Dental University (TMDU) researchers has shown a cyclic decapeptide, termed peptide 1, mimics the dimerization arm of the EGF receptor (EGFR). EGFR is involved in cellular signal transductions
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