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Solution and Solid-State Nuclear Magnetic Resonance Structural Investigations of the Antimicrobial Designer Peptide GL13K in Membranes.

Author information

Affiliations

  • 1. Université de Strasbourg/CNRS , UMR7177, Institut de Chimie, 1, rue Blaise Pascal, 67070 Strasbourg, France.
      Authors
    • Harmouche N 1
    • Aisenbrey C 1
    • Raya J 1
    • Vermeer L 1
    • Bechinger B 1
    (5 authors)
  • 2. DIBAF-University of Tuscia-Viterbo, Largo dell'Universita' , Blocco D, 01100 Viterbo, Italy.
      Authors
    • Porcelli F 2
    (1 author)
  • 3. Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota , 321 Church Street Southeast, Minneapolis, Minnesota 55455, United States.
      Authors
    • Xia Y 3
    • Nelson SED 3
    • Veglia G 3
    (3 authors)
  • 4. Minnesota Dental Research Center for Biomaterials and Biomechanics and Department of Restorative Sciences, University of Minnesota School of Dentistry , 515 Delaware Street Southeast, Minneapolis, Minnesota 55455, United States.
      Authors
    • Chen X 4
    • Aparicio C 4
    (2 authors)
  • 5. Department of Diagnostic and Biological Sciences, University of Minnesota School of Dentistry , 515 Delaware Street Southeast, Minneapolis, Minnesota 55455, United States.
      Authors
    • Gorr SU 5
    (1 author)

ORCIDs linked to this article

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Biochemistry, 01 Aug 2017, 56(32):4269-4278
https://doi.org/10.1021/acs.biochem.7b00526 PMID: 28699734 

Abstract 

The antimicrobial peptide GL13K encompasses 13 amino acid residues and has been designed and optimized from the salivary protein BPIFA2 to exhibit potent bacteriocidal and anti-biofilm activity against Gram-negative and Gram-positive bacteria as well as anti-lipopolysaccharide activity in vitro and in vivo. Here, the peptide was analyzed in a variety of membrane environments by circular dichroism spectroscopy and by high-resolution multidimensional solution nuclear magnetic resonance (NMR) spectroscopy. Whereas in the absence of membranes a random coil conformation predominates, the peptide adopts a helical structure from residue 5 to 11 in the presence of dodecylphosphocholine micelles. In contrast, a predominantly β-sheet structure was observed in the presence of lipid bilayers carrying negatively charged phospholipids. Whereas 15N solid-state NMR spectra are indicative of a partial alignment of the peptide 15N-1H vector along the membrane surface, 2H and 31P solid-state NMR spectra indicate that in this configuration the peptide exhibits pronounced disordering activities on the phospholipid membrane, which is possibly related to antimicrobial action. GL13K, thus, undergoes a number of conformational transitions, including a random coil state in solution, a helical structure upon dilution at the surface of zwitterionic membranes, and β-sheet conformations at high peptide:lipid ratios.

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Read article at publisher's site: https://doi.org/10.1021/acs.biochem.7b00526

Read article for free, from open access legal sources, via Unpaywall: https://univoak.eu/islandora/object/islandora%3A78472/datastream/PDF/viewUnpaywall

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Funding 

Funders who supported this work.

Agence Nationale de la Recherche (4)

Centre National de la Recherche Scientifique

    Fondation pour la Recherche M?dicale

      NIDCR NIH HHS (2)

      NIGMS NIH HHS (1)

      National Institute of Dental and Craniofacial Research (2)

      National Institute of General Medical Sciences (1)

      Office of the Vice President for Research, University of Minnesota (1)

      R?gion Alsace

        R?seau th?matique de recherche avanc?e

          School of Dentistry, University of Minnesota

            Universit? de Strasbourg