Probing membrane permeabilization by the antimicrobial peptide distinctin in mercury-supported biomimetic membranes. (Articolo in rivista)

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  • Probing membrane permeabilization by the antimicrobial peptide distinctin in mercury-supported biomimetic membranes. (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbamem.2011.07.033. (literal)
Alternative label
  • Becucci L, Papini M, Mullen D, Scaloni A, Veglia G, Guidelli R. (2011)
    Probing membrane permeabilization by the antimicrobial peptide distinctin in mercury-supported biomimetic membranes.
    in Biochimica et biophysica acta (Print); Elsevier, Amsterdam (Paesi Bassi)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Becucci L, Papini M, Mullen D, Scaloni A, Veglia G, Guidelli R. (literal)
Pagina inizio
  • 2745 (literal)
Pagina fine
  • 2752 (literal)
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  • http://www.sciencedirect.com/science/article/pii/S0005273611002380# (literal)
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  • 1808 (literal)
Rivista
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  • Biochim Biophys Acta. 2011 Nov;1808(11):2745-52. Epub 2011 Jul 30. (literal)
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  • 8 (literal)
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  • 11 (literal)
Note
  • PubMe (literal)
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  • Chemistry Department, Florence University, Via della Lastruccia 3, Sesto Fiorentino, I-50019 (Firenze), Italy Department of Chemistry and Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 207 Pleasant St. S.E., Minneapolis, MN 55455, USA Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, Naples, I-80147, Italy (literal)
Titolo
  • Probing membrane permeabilization by the antimicrobial peptide distinctin in mercury-supported biomimetic membranes. (literal)
Abstract
  • The mechanism of membrane permeabilization by the antimicrobial peptide distinctin was investigated by using two different mercury-supported biomimetic membranes, namely a lipid self-assembled monolayer and a lipid bilayer tethered to the mercury surface through a hydrophilic spacer (tethered bilayer lipid membrane: tBLM). Incorporation of distinctin into a lipid monolayer from its aqueous solution yields rapidly ion channels selective toward inorganic cations, such as Tl(+) and Cd(2+). Conversely, its incorporation in a tBLM allows the formation of ion channels permeable to potassium ions only at non-physiological transmembrane potentials, more negative than -340mV. These channels, once formed, are unstable at less negative transmembrane potentials. The kinetics of their formation is consistent with the disruption of distinctin clusters adsorbed on top of the lipid bilayer, incorporation of the resulting monomers and their aggregation into hydrophilic pores by a mechanism of nucleation and growth. Comparing the behavior of distinctin in tBLMs with that in conventional black lipid membranes strongly suggests that distinctin channel formation in lipid bilayer requires the partitioning of distinctin molecules between the two sides of the lipid bilayer. We can tentatively hypothesize that an ion channel is formed when one distinctin cluster on one side of the lipid bilayer matches another one on the opposite side. (literal)
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