Journal article

Melittin peptides exhibit different activity on different cells and model membranes

Elaheh Jamasbi, Steven Batinovic, Robyn A Sharples, Marc-Antoine Sani, Roy Michael Robins-Browne, John D Wade, Frances Separovic, Mohammed Akhter Hossain

AMINO ACIDS | SPRINGER WIEN | Published : 2014

Abstract

Melittin (MLT) is a lytic peptide with a broad spectrum of activity against both eukaryotic and prokaryotic cells. To understand the role of proline and the thiol group of cysteine in the cytolytic activity of MLT, native MLT and cysteine-containing analogs were prepared using solid phase peptide synthesis. The antimicrobial and cytolytic activities of the monomeric and dimeric MLT peptides against different cells and model membranes were investigated. The results indicated that the proline residue was necessary for antimicrobial activity and cytotoxicity and its absence significantly reduced lysis of model membranes and hemolysis. Although lytic activity against model membranes decreased fo..

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Grants

Awarded by Australian Research Council


Funding Acknowledgements

We acknowledge partial support of the studies undertaken in the authors' laboratory by the Australian Research Council (DP150103522) to MAH and JDW. Research at the FNI was supported by the Victorian Government's Operational Infrastructure Support Program. EJ thanks the University of Melbourne for an MIRS.