HP (2-20) derived from the amino terminal region of Helicobacter pylori ribosomal protein L1 exerts its antifungal effects by damaging the plasma membranes of Candida albicans

Dong Gun Lee, Pyoung Il Kim, Yoonkyung Park, Seung Hwan Jang, Seong Cheol Park, Eun Rhan Woo, Kyung Soo Hahm

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

The fungicidal effects of the peptide HP (2-20), derived from the N-terminal sequence of Helicobacter pylori ribosomal protein L1 (RPL1), have been investigated. HP (2-20) displays a strong fungicidal activity against various fungi, without haemolytic activity against human erythrocyte cells, and the fungicidal activity is inhibited by Ca2+ and Mg2+ ions. In order to investigate the fungicidal mechanism(s) of HP (2-20), the amount of intracellular trehalose was measured in C. albicans. It was found that the amounts of intracellular trehalose were decreased when HP (2-20) was used. The action of the peptide against fungal cell membranes was further examined by the potassium-release test; HP (2-20) was found to increase the amount of K+ released from the cells. Furthermore, HP (2-20) caused significant morphological changes, as shown by scanning electron microscopy, and by testing the membrane disrupting activity using liposomes (phosphatidyl choline/cholesterol; 10: 1, w/w). Our results suggest that HP (2-20) may exert its antifungal activity by disrupting the structure of cell membranes, via pore formation or direct interaction with the lipid bilayers.

Original languageEnglish
Pages (from-to)453-460
Number of pages8
JournalJournal of Peptide Science
Volume8
Issue number8
DOIs
StatePublished - 2002

Keywords

  • Antifungal activity
  • Fungicidal mechanism
  • HP (2-20)
  • Potassium-release test

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