Journal article
Selective Acylation Enhances Membrane Charge Sensitivity of the Antimicrobial Peptide Mastoparan-X
Colloids and Biological Interfaces Group, Self-organizing materials for nanotechnology Section, Department of Micro- and Nanotechnology, Technical University of Denmark1
Self-organizing materials for nanotechnology Section, Department of Micro- and Nanotechnology, Technical University of Denmark2
Department of Micro- and Nanotechnology, Technical University of Denmark3
Biomedical Tracers, Radiation Research Division, Risø National Laboratory for Sustainable Energy, Technical University of Denmark4
Radiation Research Division, Risø National Laboratory for Sustainable Energy, Technical University of Denmark5
Risø National Laboratory for Sustainable Energy, Technical University of Denmark6
Organic Chemistry, Department of Chemistry, Technical University of Denmark7
Department of Chemistry, Technical University of Denmark8
The partitioning of the wasp venom peptide mastoparan-X (MPX) into neutral and negatively charged lipid membranes has been compared with two new synthetic analogs of MPX where the Nα-terminal of MPX was acylated with propanoic acid (PA) and octanoic acid (OA). The acylation caused a considerable change in the membrane partitioning properties of MPX and it was found that the shorter acylation with PA gave improved affinity and selectivity toward negatively charged membranes, whereas OA decreased the selectivity.
Based on these findings, we hypothesize that minor differences in the embedding and positioning of the peptide in the membrane caused by either PA or OA acylation play a critical role in the fine-tuning of the effective charge of the peptide and thereby the fine-tuning of the peptide's selectivity between neutral and negatively charged lipid membranes.
This finding is unique compared to previous reports where peptide acylation enhanced membrane affinity but also resulted in impaired selectivity. Our result may provide a method of enhancing selectivity of antimicrobial peptides toward bacterial membranes due to their high negative charge—a finding that should be investigated for other, more potent antimicrobial peptides in future studies.
Language: | English |
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Publisher: | The Biophysical Society |
Year: | 2011 |
Pages: | 399-409 |
ISSN: | 21530378 , 2153036x , 15420086 , 00063495 and 05236800 |
Types: | Journal article |
DOI: | 10.1016/j.bpj.2010.11.040 |
ORCIDs: | Henriksen, Jonas Rosager , Clausen, Mads Hartvig and Andresen, Thomas Lars |