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Cell penetrating peptides and cationic antibacterial peptides: two sides of the same coin.

ABSTRACT: 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.

SUBMITTER: Rodriguez Plaza JG

PROVIDER: S-EPMC4031501 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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Cell penetrating peptides and cationic antibacterial peptides: two sides of the same coin.

Rodriguez Plaza Jonathan G JG Morales-Nava Rosmarbel R Diener Christian C Schreiber Gabriele G Gonzalez Zyanya D ZD Lara Ortiz Maria Teresa MT Ortega Blake Ivan I Pantoja Omar O Volkmer Rudolf R Klipp Edda E Herrmann Andreas A Del Rio Gabriel G

The Journal of biological chemistry 20140405 21

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, incl ...[more]

PMID: 24706763

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