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J Biol Chem. 2014 May 23;289(21):14448-57. doi: 10.1074/jbc.M113.515023. Epub 2014 Apr 5.

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

Author information

1
From the Biochemistry and Structural Biology Department, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Circuito Exterior S/N Ciudad Universitaria, 04510 México D.F., México.
2
Materials science and biophysics department, Instituto de Ciencias Fisicas, Universidad Nacional Autónoma de México, Av. Universidad S/N, Col. Chamilpa, 62210 Cuernavaca, Morelos, México.
3
Instituto de Biotecnología, Universidad Nacional Autónoma de México, A.P. 510-3, Colonia Miraval, Cuernavaca, Morelos, México 62250.
4
Institut für Medizinische Immunologie, Charité-Universitätsmedizin Berlin, Hessische Strasse 3-4, 10117 Berlin and Leibniz-Institut für Molekulare Pharmakologie, Robert-Roessle Strasse 10, 13125 Berlin, Germany, and.
5
Theoretische und Molekulare Biophysik, Humboldt-Universität zu Berlin, Invalidenstrasse 42, 10115 Berlin, Germany.
6
From the Biochemistry and Structural Biology Department, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Circuito Exterior S/N Ciudad Universitaria, 04510 México D.F., México, gdelrio@ifc.unam.mx.

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.

KEYWORDS:

Antimicrobial Peptides; Cell-penetrating Peptides; Computational Biology; Membrane Biophysics; Receptor Endocytosis

PMID:
24706763
PMCID:
PMC4031501
DOI:
10.1074/jbc.M113.515023
[Indexed for MEDLINE]
Free PMC Article

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