The membrane insertion of helical antimicrobial peptides from the N-terminus of Helicobacter pylori ribosomal protein L1

Tzong-Hsien Lee, Kristopher Norman Hall, Marcus J Swann, Jonathan Popplewell, Sharon Unabia, Yoonkyung Park, Kyung-Soo Hahm, Marie Isabel Aguilar

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Abstract

The interaction of two helical antimicrobial peptides, HPA3 and HPA3P with planar supported lipid membranes was quantitatively analysed using two complementary optical biosensors. The peptides are analogues of Hp(2-20) derived from the N-terminus of Helicobacter pylori ribosomal protein L1 (RpL1). The binding of these two peptide analogues to zwitterionic dimyristoyl-phosphatidylcholine (DMPC) and negatively charged membranes composed of DMPC/dimyristoylphosphatidylglycerol (DMPG) (4:1) was determined using surface plasmon resonance (SPR) and dual polarisation interferometry (DPI). Using SPR analysis, it was shown that the proline substitution in HPA3P resulted in much lower binding for both zwitterionic and anionic membranes than HPA3. Structural changes in the planar DMPC and DMPC/DMPG (4:1) bilayers induced by the binding of both Hp(2-20) analogues were then resolved in real-time with DPI.....
Original languageEnglish
Pages (from-to)544 - 557
Number of pages14
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1798
Issue number3
DOIs
Publication statusPublished - 2010

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