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• W2021122013 abstract "In a previous study, we determined that HP(2–20) (residues 2–20 of parental HP derived from the N-terminus of Helicobacter pylori Ribosomal Protein L1) and its analogue, HPA3, exhibit broad-spectrum antimicrobial activity. The primary objective of the present study was to gain insight into the relevant mechanisms of action using analogues of HP(2–20) together with model liposomes of various lipid compositions and electron microscopy. We determined that these analogues, HPA3 and HPA3NT3, exert potent antibacterial effects in low-salt buffer and antifungal activity against chitin-containing fungi, while having little or no hemolytic activity or cytotoxicity against mammalian cell lines. Our examination of the interaction of HP(2–20) and its analogues with liposomes showed that the peptides disturb both neutral and negatively-charged membranes, as demonstrated by the release of encapsulated fluorescent markers. The release of fluorescent markers induced by HP(2–20) and its analogues was inversely related to marker size. The pore created by HP(2–20) shows that the radius is approximately 1.8 nm, whereas HPA3, HPA3NT3, and melittin have apparent radii between 3.3 and 4.8 nm. Finally, as shown by electron microscopy, the liposomes and various microbial cells treated with HPA3 and HPA3NT3 showed oligomerization and blebbing similar to that seen with melittin, while HP(2–20) exhibited flabbiness. These results suggest that HP(2–20) may exert its antibiotic effects through a small pore (about 1.8 nm), whereas HPA3 and HPA3NT3 formed pores of a size consistent with those formed by melittin." @default.
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• W2021122013 date "2008-01-01" @default.
• W2021122013 modified "2023-10-18" @default.
• W2021122013 title "Amphipathic α-helical peptide, HP (2–20), and its analogues derived from Helicobacter pylori: Pore formation mechanism in various lipid compositions" @default.
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• W2021122013 doi "https://doi.org/10.1016/j.bbamem.2007.09.020" @default.
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