Cell Penetrating Peptides and Cationic Antibacterial Peptides: two sides of the same coin (original) (raw)
2014, Journal of Biological Chemistry
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Cell Penetrating Peptides and Cationic Antibacterial Peptides
Journal of Biological Chemistry, 2014
Background: Iztli peptides (IP) are a new class of antibacterial peptides that could be internalized by receptor-mediated endocytosis in yeast. Results: IP-1 penetrates cells independently of endocytosis and makes pores in membranes with large electric potential. Conclusion: Antibacterial peptides like IP-1 make pores or penetrate membranes depending on the membrane potential. Significance: Antibacterial peptides with penetrating activity are robust to control bacterial infections. Cell penetrating peptides (CPP) and cationic antibacterial peptides (CAP) have similar physicochemical properties and yet it is not understood how such similar peptides display different activities. To address this question, we used Iztli peptide 1 (IP-1) because it has both CPP and CAP activities. Combining experimental and computational modeling of the internalization of IP-1, we show it is not internalized by receptor-mediated endocytosis, yet it permeates into many different cell types, including fungi and human cells. We also show that IP-1 makes pores in the presence of high electrical potential at the membrane, such as those found in bacteria and mitochondria. These results provide the basis to understand the functional redundancy of CPPs and CAPs.
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