Amphiphilic Poly(phenyleneethynylene)s Can Mimic Antimicrobial Peptide Membrane Disordering Effect by Membrane Insertion.

Antimicrobial peptides (AMPs) are a class of peptides that are innate to various organisms and function as a defense agent against harmful microorganisms by means of membrane disordering. Characteristic chemical and structural properties of AMPs allow selective interaction and subsequent disruption...

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Publicado en:Journal of the American Chemical Society Vol. 128; no. 40; pp. 13123 - 13130
Autores principales: Ishitsuka, Yuji, Arnt, Lachelle, Majewski, Jaroslaw, Frey, Shelli, Ratajczek, Maria, Kjaer, Kristian, Tew, Gregory N., Lee, Ka Yee C.
Formato: Artículo
Publicado: American Chemical Society 10/11/2006
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Acceso en línea:Ver este registro en EBSCOhost
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      dt: 10/11/2006
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      pub: American Chemical Society
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        10.1021/ja061186q
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        atl: Amphiphilic Poly(phenyleneethynylene)s Can Mimic Antimicrobial Peptide Membrane Disordering Effect by Membrane Insertion.
      aug:
        au:
          Ishitsuka, Yuji
          Arnt, Lachelle
          Majewski, Jaroslaw
          Frey, Shelli
          Ratajczek, Maria
          Kjaer, Kristian
          Tew, Gregory N.
          Lee, Ka Yee C.
        affil:
          Department of Chemistry, the Institute for Biophysical Dynamics & the James Franck Institute, the University of Chicago, Chicago, Illinois 60637
          Department of Polymer Science and Engineering, University of Massachusetts, Amherst, Amherst, Massachusetts 01003
          Manuel Lujan, Jr. Neutron Scattering Center, Los Alamos National Laboratory, Los Alamos, New Mexico 87545
          Materials Research Department, Niels Bohr Institute, University of Copenhagen, DK-2100 Copenhagen, Denmark
      su:
        Antimicrobial peptides
        Organisms
        Cell membranes
        Polymers
        Optical diffraction
      sug:
        subj:
          Antimicrobial peptides
          Organisms
          Cell membranes
          Polymers
          Optical diffraction
      ab: Antimicrobial peptides (AMPs) are a class of peptides that are innate to various organisms and function as a defense agent against harmful microorganisms by means of membrane disordering. Characteristic chemical and structural properties of AMPs allow selective interaction and subsequent disruption of invaders' cell membranes. Polymers based on m-phenylene ethynylenes (mPE) were designed and synthesized to mimic the amphiphilic, cationic, and rigid structure of AMPs and were found to be good mimics of AMPs in terms of their high potency toward microbes and low hemolytic activities. Using a Langmuir monolayer insertion assay, two mPEs are found to readily insert into anionic model bacterial membranes but to differ in the degree of selectivity between bacterial and mammalian erythrocyte model membranes. Comparison of grazing incidence X-ray diffraction (GIXD) data before and after the insertion of mPE clearly indicates that the insertion of mPE disrupts lipid packing, altering the tilt of the lipid tail. X-ray reflectivity (XR) measurements of the lipid/mPE system demonstrate that mPE molecules insert through the headgroup region and partially into the tail group region, thus accounting for the observed disordering of tail packing. This study demonstrates that mPEs can mimic AMP's membrane disordering.
      pubtype: Academic Journal
      doctype: Article
      src: R
    language: English
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