Abstract
Antimicrobial peptides (AMPs), or host defense peptides, are small cationic or amphipathic molecules produced by prokaryotic and eukaryotic organisms that play a key role in the innate immune defense against viruses, bacteria and fungi. AMPs have either antimicrobial or anticancer activities. Indeed, cationic AMPs are able to disrupt microbial cell membranes by interacting with negatively charged phospholipids. Moreover, several peptides are capable to trigger cytotoxicity of human cancer cells by binding to negatively charged phosphatidylserine moieties which are selectively exposed on the outer surface of cancer cell plasma membranes. In addition, some AMPs, such as LTX-315, have shown to induce release of tumor antigens and potent damage associated molecular patterns by causing alterations in the intracellular organelles of cancer cells. Given the recognized medical need of novel anticancer drugs, AMPs could represent a potential source of effective therapeutic agents, either alone or in combination with other small molecules, in oncology. In this review we summarize and describe the properties and the mode of action of AMPs as well as the strategies to increase their selectivity toward specific cancer cells.
Highlights
Antimicrobial peptides (AMPs) are short amino acid sequences produced by all organisms, from bacteria to mammals, which act as primary defense against a broad spectrum of pathogens [1]
Dermaseptins (DRS) are polycationic peptides isolated from Phyllomedusa frogs that are effective against bacteria, parasites, protozoa, viruses, and cancer cells in vitro
R-Tf-D-LP4 (KWTWKNSNGATWALNVATELKKEWTWSHRPYIAH) is a cell-penetrating peptide derived from the voltage-dependent anion channel 1 (VDAC1), which is a beta-barrel protein located in the outer mitochondrial membrane
Summary
Antimicrobial peptides (AMPs) are short amino acid sequences produced by all organisms, from bacteria to mammals, which act as primary defense against a broad spectrum of pathogens [1]. AMPs are short peptides, mostly less than 100 amino acids long, that in general do not share conserved motifs but are characterized by net positive charges and high proportions of hydrophobic residues [19]. As a result, they tend to establish non-specific interactions with negatively charged phospholipids, such as the phosphatidylglycerol, that are abundant in the microbial membranes causing increased permeability, leakage of cytoplasmic components and cell death [20,21,22,23]. We summarize the methods used to increase their anticancer activity
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