Antimicrobial Peptides and Their Superior Fluorinated Analogues: Structure-Activity Relationships as Revealed by NMR Spectroscopy and MD Calculations

  1. Díaz, M.D. 1
  2. Palomino-Schätzlein, M. 2
  3. Corzana, F. 3
  4. Andreu, C. 4
  5. Carbajo, R.J. 2
  6. Del Olmo, M. 4
  7. Canales-Mayordomo, A. 5
  8. Pineda-Lucena, A. 2
  9. Asensio, G. 4
  10. Jiménez-Barbero, J. 1
  1. 1 Centro de Investigaciones Biológicas
    info

    Centro de Investigaciones Biológicas

    Madrid, España

    ROR https://ror.org/04advdf21

  2. 2 Centro de Investigación Príncipe Felipe
    info

    Centro de Investigación Príncipe Felipe

    Valencia, España

    ROR https://ror.org/05xr2yq54

  3. 3 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

  4. 4 Universitat de València
    info

    Universitat de València

    Valencia, España

    ROR https://ror.org/043nxc105

  5. 5 Universidad Complutense de Madrid
    info

    Universidad Complutense de Madrid

    Madrid, España

    ROR 02p0gd045

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Journal:
Chembiochem : a European journal of chemical biology

ISSN: 1439-4227

Year of publication: 2010

Volume: 11

Issue: 17

Pages: 2424-2432

Type: Article

DOI: 10.1002/CBIC.201000424 PMID: 21077089 SCOPUS: 2-s2.0-78649261564 WoS: WOS:000284718100014 GOOGLE SCHOLAR

More publications in: Chembiochem : a European journal of chemical biology

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Abstract

The conformations of two synthetic pentapeptides with antimicrobial activity and their 4-fluorophenylalanine (Pff)-containing analogues (ArXArXAr-NH 2; Ar=Phe, Pff; X=Lys, Arg) have been studied. NMR experiments carried out both in aqueous fluoroalcohol solutions and SDS micelles permitted their interactions with membrane-like environments to be explored. WaterLOGSY experiments and Mn 2+-based paramagnetic probes were also applied to assess their orientations with respect to the SDS micelles. In addition, pulse-field gradient (PFG) diffusion NMR spectroscopy studies were conducted, under different experimental conditions (i.e., concentration, temperature) to characterize the possible changes in the peptides' aggregation states as a putative critical factor for their antimicrobial activity. Finally, molecular dynamics simulations on a variety of conformations showed the intrinsic flexibility of these peptides in both aqueous solutions and membrane-mimetic systems.A flexible friend? The interactions of antimicrobial peptides with membrane-mimetic media have been studied under different conditions by NMR spectroscopy and molecular dynamics simulations. Experiments were carried out to determine the conformations, orientations, and aggregation states of two synthetic pentapeptides and their 4-fluorophenylalanine-containing analogues in aqueous fluoroalcohol solutions and in SDS micelles. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.