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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ekblad, Bie Kaznessis, Yiannis N. Kyriakou, Panagiota K. Kristiansen, Per Eugen |
| Description | Author Affiliation: Kyriakou PK ( Department of Chemical Engineering and Materials Science, University of Minnesota, Minneapolis, MN 55455, United States.); Ekblad B ( Department of Biosciences, University of Oslo, Post box 1041 Blindern, 0316 Oslo, Norway.); Kristiansen PE ( Department of Biosciences, University of Oslo, Post box 1041 Blindern, 0316 Oslo, Norway.); Kaznessis YN ( Department of Chemical Engineering and Materials Science, University of Minnesota, Minneapolis, MN 55455, United States. Electronic address: yiannis@umn.edu.) |
| Abstract | The emergence of antibiotic resistant microorganisms poses an alarming threat to global health. Antimicrobial peptides (AMPs) are considered a possible effective alternative to conventional antibiotic therapies. An understanding of the mechanism of action of AMPs is needed in order to better control and optimize their bactericidal activity. Plantaricin EF is a heterodimeric AMP, consisting of two peptides Plantaricin E (PlnE) and Plantaricin F (PlnF). We studied the behavior of these peptides on the surface of a model lipid bilayer. We identified the residues that facilitate peptide–peptide interactions. We also identified residues that mediate interactions of the dimer with the membrane. PlnE interacts with the membrane through amino acids at both its termini, while only the N terminus of PlnF approaches the membrane. By comparing the activity of single-site mutants of the two-peptide bacteriocin and the simulations of the bacteriocin on the surface of a model lipid bilayer, structure activity relationships are proposed. These studies allow us to generate hypotheses that relate biophysical interactions observed in simulations with the experimentally measured activity. We find that single-site amino acid substitutions result in markedly stronger antimicrobial activity when they strengthen the interactions between the two peptides, while, concomitantly, they weaken peptide–membrane association. This effect is more pronounced in the case of the PlnE mutant (G20A), which interacts the strongest with PlnF and the weakest with the membrane while displaying the highest activity. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1858 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Antimicrobial Cationic Peptides Chemistry Bacteriocins Cell Membrane Lipid Bilayers Amino Acids Anti-Bacterial Agents Pharmacology Metabolism Drug Effects Molecular Dynamics Simulation Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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