Interaction of the Antimicrobial Peptide PGLa and Its Ala-Substitution Analog with Membrane-Mimetic Systems

  • Sylvie E. Blondelle
  • Karl Lohner
Part of the American Peptide Symposia book series (APSY, volume 7)


The rapid emergence of multi-resistant bacteria poses a major global health problem and calls for the development of antibiotics that bacteria have never seen before. The discovery of host defense peptides has opened new avenues for developing such drugs. Many of these peptides, while exhibiting random structure in solution, adopt an α-helical conformation upon interaction with cell membranes and model membranes [1]. However, synthetic α-helical peptides are often toxic to mammalian cells. A better understanding of the biophysical requirements for selective bacterial lysis to occur in regards to peptide induced structures, as well as their effect on lipid properties, is therefore needed for the de novo design of novel antimicrobial peptides. Using synthetic peptides having varying hydrophobic/hydrophilic amino acid distribution, we have investigated how a peptide’s helicity and hydrophobicity affect its interaction with model membrane systems and how this correlates with the peptide activity.


Antimicrobial Peptide Hemolytic Activity Small Unilamellar Vesicle Amino Acid Distribution Major Global Health Problem 
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Copyright information

© Springer Science+Business Media Dordrecht 2001

Authors and Affiliations

  • Sylvie E. Blondelle
    • 1
  • Karl Lohner
    • 2
  1. 1.Torrey Pines Institute for Molecular StudiesSan DiegoUSA
  2. 2.Institut fûr Biophysik und RõntgenstrukturforschungÕsterreichische Akademie der WissenschaftenGrazAustria

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