Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism
AuthorSani, M.-A.; Whitwell, T. C.; Gehman, J. D.; Robins-Browne, R. M.; Attard, T. J.; Reynolds, E. C.; O’Brien-Simpson, N. M.; Separovica, F.
Source TitleAntimicrobial Agents and Chemotherapy
PublisherAmerican Society for Microbiology
University of Melbourne Author/sSani, Marc Antoine; WHITWELL, THOMAS; GEHMAN, JOHN; Robins-Browne, Roy; Attard, Troy; Reynolds, Eric; O'Brien-Simpson, Neil; Separovic, Frances; PANTARAT, NAMFON
AffiliationDepartment of Microbiology and Immunology
Oral Health CRC, Melbourne Dental School
Microbiology & Immunology
Melbourne Dental School
Document TypeJournal Article
CitationsSani, M., Whitwell, T. C., Gehman, J. D., Robins-Browne, R. M., Attard, T. J., Reynolds, E. C., et al. (2013). Maculatin 1.1 disrupts Staphylococcus aureus lipid membranes via a pore mechanism. Antimicrobial Agents and Chemotherapy, 57(8), 3593-3600.
Access StatusThis item is currently not available from this repository
NHMRC Grant codeNHMRC/1008106
The research outputs in this collection have been funded in whole or in part by the National Health and Medical Research Council (NHMRC)
Copyright © 2013, American Society for Microbiology. All Rights Reserved.
Maculatin 1.1 (Mac1) showed potent activity against Staphylococcus aureus with an MIC of 7 _M. The mode of action of Mac1 was investigated by combining assays with S. aureus cells and lipid vesicles mimicking their membrane composition. A change in Mac1 conformation was monitored by circular dichroism from random coil to ca. 70% _-helix structure in contact with vesicles. Electron micrographs of S. aureus incubated with Mac1 showed rough and rippled cell surfaces. An uptake of 65% of small (FD, 4 kDa [FD-4]) and 35% of large (RD, 40 kDa [RD-40]) fluorescent dextrans by S. aureus was observed by flow cytometry and indicate that Mac1 formed a pore of finite size. In model membranes with both dyes encapsulated together, the full release of FD-4 occurred, but only 40% of RD-40 was reached, supporting the flow cytometry results, and indicating a pore size between 1.4 and 4.5 nm. Finally, solid-state nuclear magnetic resonance showed formation of an isotropic phase signifying highly mobile lipids such as encountered in a toroidal pore structure. Overall, Mac1 is a promising antimicrobial peptide with the potent capacity to form pores in S. aureus membranes.
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