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Effects of peptide hydrophobicity on its incorporation in phospholipid membranes - an NMR and ellipsometry study
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2011 (English)In: Biochimica et Biophysica Acta, ISSN 0006-3002, Vol. 1808, no 1, 244-252 p.Article in journal (Refereed) Published
Abstract [en]

Effects of peptide hydrophobicity on lipid membrane binding, incorporation, and defect formation was investigated for variants of the complement-derived antimicrobial peptide CNY21 (CNYITELRRQHARASHLGLAR), in anionic 1-palmitoyl-2-oleoylphosphatidylethanolamine (POPE)/1-palmitoyl-2-oleoylphosphatidylglycerol (POPG) and zwitterionic 1-palmitoyl-2-oleoylphosphatidylcholine (POPC) membranes. Using a method combination of, e.g., ellipsometry, CD, and fluorescence spectroscopy, it was shown that peptide adsorption, as well as peptide-induced liposome leakage and bactericidal potency against Escherichia coli and Pseudomonas aeruginosa, was promoted by increasing the hydrophobicity of CNY21 through either substituting the two histidines (H) in CNY21 with more hydrophobic leucine (L) residues, or end-tagging with tritryptophan (WWW). Fluorescence spectroscopy revealed that both CNY21WWW and the WWW tripeptide localized to the polar headgroup region of these phospholipid membranes. Deuterium NMR experiments on macroscopically oriented membranes containing fully (palmitoyl) deuterated POPC (POPC-d(31)) demonstrated that both CNY21L and CNY21WWW induced disordering of the lipid membrane. In contrast, for cholesterol-supplemented POPC-d(31) bilayers, peptide-induced disordering was less pronounced in the case of CNY21L, indicating that the peptide is unable to partition to the interior of the lipid membrane in the presence of cholesterol. CNY21WWW, on the other hand, retained its membrane-disordering effect also for cholesterol-supplemented POPC-d(31). These findings were supported by pulsed field gradient NMR experiments where the lateral lipid diffusion was determined in the absence and presence of peptides. Overall, the results provide some mechanistic understanding to previously observed effects of peptide hydrophobization through point mutations and end-tagging, particularly so for complement-based antimicrobial peptides.

Place, publisher, year, edition, pages
2011. Vol. 1808, no 1, 244-252 p.
Keyword [en]
AMP, antimicrobial peptide, ellipsometry, liposome, membrane, NMR
URN: urn:nbn:se:umu:diva-38791DOI: 10.1016/j.bbamem.2010.08.015PubMedID: 20801096OAI: diva2:382642
Available from: 2011-01-03 Created: 2010-12-30 Last updated: 2011-01-05Bibliographically approved

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Orädd, Greger
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