Literature DB >> 10556525

Voltage-dependent interaction of the peptaibol antibiotic zervamicin II with phospholipid vesicles.

T N Kropacheva1, J Raap.   

Abstract

The effect of a transmembrane potential on ion channel formation by zervamicin II (ZER-II) was studied in a vesicular model system. The dissipation of diffusion potential caused by addition of ZER-II to small phosphatidylcholine vesicles was monitored using fluorescent (Safranine T) and optical (Oxonol YI) probes. Cis-positive potentials facilitated channel formation, while at cis-negative potentials, ion fluxes were inhibited. A potential-independent behavior of ZER-II was observed at high peptide concentrations, most likely due to its membrane modifying property.

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Year:  1999        PMID: 10556525     DOI: 10.1016/s0014-5793(99)01401-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Spatial structure of zervamicin IIB bound to DPC micelles: implications for voltage-gating.

Authors:  Z O Shenkarev; T A Balashova; R G Efremov; Z A Yakimenko; T V Ovchinnikova; J Raap; A S Arseniev
Journal:  Biophys J       Date:  2002-02       Impact factor: 4.033

2.  Modeling the secondary structures of the peptaibols antiamoebin I and zervamicin II modified with D-amino acids and proline analogues.

Authors:  Tarsila G Castro; Nuno M Micaêlo; Manuel Melle-Franco
Journal:  J Mol Model       Date:  2017-10-16       Impact factor: 1.810

3.  Peptaibol zervamicin IIb structure and dynamics refinement from transhydrogen bond J couplings.

Authors:  Z O Shenkarev; T A Balashova; Z A Yakimenko; T V Ovchinnikova; A S Arseniev
Journal:  Biophys J       Date:  2004-06       Impact factor: 4.033

  3 in total

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