4.5 Article

Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells

期刊

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1808, 期 10, 页码 2581-2590

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.06.007

关键词

CAMPs; KLK; Sialic acids; Plasma membrane accumulation

资金

  1. Austrian Research Promotion Agency
  2. Austrian Science Fund (FWF) [Y250-B03]
  3. Intercell AG
  4. Austrian Science Fund (FWF) [Y250] Funding Source: Austrian Science Fund (FWF)
  5. Austrian Science Fund (FWF) [Y 250] Funding Source: researchfish

向作者/读者索取更多资源

Cationic antimicrobial peptides (CAMPS) selectively target bacterial membranes by electrostatic interactions with negatively charged lipids. It turned out that for inhibition of microbial growth a high CAMP membrane concentration is required, which can be realized by the incorporation of hydrophobic groups within the peptide. Increasing hydrophobicity, however, reduces the CAMP selectivity for bacterial over eukaryotic host membranes, thereby causing the risk of detrimental side-effects. In this study we addressed how cationic amphipathic peptides in particular a CAMP with Lysine-Leucine-Lysine repeats (termed KLK) affect the localization and dynamics of molecules in eukaryotic membranes. We found KLK to selectively inhibit the endocytosis of a subgroup of membrane proteins and lipids by electrostatically interacting with negatively charged sialic acid moieties. Ultrastructural characterization revealed the formation of membrane invaginations representing fission or fusion intermediates, in which the sialylated proteins and lipids were immobilized. Experiments on structurally different cationic amphipathic peptides (KLK, 6-MO-LF11-322 and NK14-2) indicated a cooperation of electrostatic and hydrophobic forces that selectively arrest sialylated membrane constituents. (C) 2011 Elsevier B.V. All rights reserved.

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