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Insights Into the Mechanism of Action of Two Analogues of Aurein 2.2 by Raheem, Nigare; Kumar, Prashant; Lee, Ethan; Cheng, John T.J.; Hancock, Robert E.W.; Straus, Suzana K. is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The naturally occurring host defense peptide (HDP), aurein 2.2, secreted by the amphibian Litoria aurea, acts as a moderate antibacterial, affecting Gram positive bacteria such as Staphylococcus aureus by forming selective ion pores. In a quest to find more active analogues of aurein 2.2, peptides 73 and 77 were discovered. These peptides were rich in arginine and tryptophan and found to have MICs of 4 μg/mL. Here we examined what impact the increased charge from +2 to +3 and a slight increase in hydrophobic moment relative to aurein 2.2 had on the mechanism of action of these two analogues. Using a time-kill assay, both peptides 73 and 77 were found to kill bacteria more effectively than the parent peptide. Using solution CD and NMR, the peptides were found to not adopt a continuous α-helical structure, i.e. the analogues were not helical from residue 1-13 like the parent peptide. Results obtained from oriented CD (OCD), DiSC5 and pyranine assays and a gel retardation experiment showed that the peptides did not function by membrane perturbation and further showed that peptide 73 and 77 did not interact with DNA. Overall, the data were consistent with these peptides acting as cell

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Author

Raheem, Nigare; Kumar, Prashant; Lee, Ethan; Cheng, John T.J.; Hancock, Robert E.W.; Straus, Suzana K.

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0005-2736)

Published

2020

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)