Title: | Cell penetrating peptides and cationic antibacterial peptides: two sides of the same coin |
Author(s): | Rodriguez Plaza JG; Morales-Nava R; Diener C; Schreiber G; Gonzalez ZD; Lara Ortiz MT; Ortega Blake I; Pantoja O; Volkmer R; Klipp E; Herrmann A; Del Rio G; |
Address: | "From the Biochemistry and Structural Biology Department, Instituto de Fisiologia Celular, Universidad Nacional Autonoma de Mexico, Circuito Exterior S/N Ciudad Universitaria, 04510 Mexico D.F., Mexico. Materials science and biophysics department, Instituto de Ciencias Fisicas, Universidad Nacional Autonoma de Mexico, Av. Universidad S/N, Col. Chamilpa, 62210 Cuernavaca, Morelos, Mexico. Instituto de Biotecnologia, Universidad Nacional Autonoma de Mexico, A.P. 510-3, Colonia Miraval, Cuernavaca, Morelos, Mexico 62250. Institut fur Medizinische Immunologie, Charite-Universitatsmedizin Berlin, Hessische Strasse 3-4, 10117 Berlin and Leibniz-Institut fur Molekulare Pharmakologie, Robert-Roessle Strasse 10, 13125 Berlin, Germany, and. Theoretische und Molekulare Biophysik, Humboldt-Universitat zu Berlin, Invalidenstrasse 42, 10115 Berlin, Germany. From the Biochemistry and Structural Biology Department, Instituto de Fisiologia Celular, Universidad Nacional Autonoma de Mexico, Circuito Exterior S/N Ciudad Universitaria, 04510 Mexico D.F., Mexico, gdelrio@ifc.unam.mx" |
ISSN/ISBN: | 1083-351X (Electronic) 0021-9258 (Print) 0021-9258 (Linking) |
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: | Algorithms Amino Acid Sequence Anti-Bacterial Agents/chemistry/metabolism/*pharmacology Antimicrobial Cationic Peptides/chemistry/pharmacokinetics/*pharmacology Cell Membrane/drug effects/metabolism Cell-Penetrating Peptides/chemistry/pharmacokinetics/*ph; |
Notes: | "MedlineRodriguez Plaza, Jonathan G Morales-Nava, Rosmarbel Diener, Christian Schreiber, Gabriele Gonzalez, Zyanya D Lara Ortiz, Maria Teresa Ortega Blake, Ivan Pantoja, Omar Volkmer, Rudolf Klipp, Edda Herrmann, Andreas Del Rio, Gabriel eng Research Support, Non-U.S. Gov't 2014/04/08 J Biol Chem. 2014 May 23; 289(21):14448-57. doi: 10.1074/jbc.M113.515023. Epub 2014 Apr 5" |