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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jcsc/119/02/0135-0140

    • Keywords

       

      Gramicidins; ion channels; wavelength-dependent fluorescence; wavelength-selective fluorescence; red-edge excitation shift.

    • Abstract

       

      Gramicidins are linear peptides that form ion channels that are specific for monovalent cations in membranes. The tryptophan residues in the gramicidin channel play a crucial role in the organization and function of the channel. The natural mixture of gramicidins, denoted as gramicidin A', consists of mostly gramicidin A, but also contains gramicidins B, C and D as minor components. We have previously shown that the tryptophan residues in ion channels formed by the naturally occurring peptide, gramicidin A', display wavelength-dependent fluorescence characteristics due to the motionally restricted environment in which they are localized. In order to check the influence of ground-state heterogeneity in the observed wavelength-selective fluorescence of gramicidin A' in membranes, we performed similar experiments with pure gramicidin A in model membranes. Our results show that the observed wavelength-selective fluorescence characteristics of naturally occurring gramicidin A' are not due to groundstate heterogeneity.

    • Author Affiliations

       

      Amitabha Chattopadhyay1 Satinder S Rawat2

      1. Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007
      2. 364 Plantation Street, Room 570R, Lazare Research Building, University of Massachusetts Medical School, Worcester, MA 01605, USA
    • Dates

       
  • Journal of Chemical Sciences | News

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