Biochimica et Biophysica Acta (BBA) - Biomembranes, Vol. 1715, Issue 1 , 30 August 2005, Pages 6-18

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Membrane association and activity of 15/16-membered peptide antibiotics: Zervamicin IIB, ampullosporin A and antiamoebin I
 Tạp chí Biochimica et Biophysica Acta (BBA) - Biomembranes 2005 Aug. 30; 1715 (1):6-18
 Tác giả   T.N. Kropachevaaa, E.S. Salnikovbb, H.-H. Nguyencc, S. Reissmanncc, Z.A. Yakimenkodd, A.A. Tagaevdd, T.V. Ovchinnikovadd and J. Raapee
 Nơi thực hiện   a Chemistry Department, Udmurt State University, Izhevsk, Russia

bInstitute of Chemical Kinetics and Combustion, Academy of Sciences, Novosibirsk, Russia

cInstitute of Biochemistry and Biophysics, Friedrich-Schiller-University, Jena, Germany

dShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia

eLeiden Institute of Chemistry, Gorlaeus Laboratories, University of Leiden, P.O. Box 9502, 2300RA, Leiden, The Netherlands

 Từ khóa   Peptaibol; Bilayer; Conductance; Channel formation; Transmembrane; Amphipathicity
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English

Permeabilization of the phospholipid membrane, induced by the antibiotic peptides zervamicin IIB (ZER), ampullosporin A (AMP) and antiamoebin I (ANT) was investigated in a vesicular model system. Membrane-perturbing properties of these 15/16 residue peptides were examined by measuring the K+ transport across phosphatidyl choline (PC) membrane and by dissipation of the transmembrane potential. The membrane activities are found to decrease in the order ZER > AMP >> ANT, which correlates with the sequence of their binding affinities. To follow the insertion of the N-terminal Trp residue of ZER and AMP, the environmental sensitivity of its fluorescence was explored as well as the fluorescence quenching by water-soluble (iodide) and membrane-bound (5- and 16-doxyl stearic acids) quenchers. In contrast to AMP, the binding affinity of ZER as well as the depth of its Trp penetration is strongly influenced by the thickness of the membrane (diC16:1PC, diC18:1PC, C16:0/C18:1PC, diC20:1PC). In thin membranes, ZER shows a higher tendency to transmembrane alignment. In thick membranes, the in-plane surface association of these peptaibols results in a deeper insertion of the Trp residue of AMP which is in agreement with model calculations on the localization of both peptide molecules at the hydrophilic–hydrophobic interface. The observed differences between the membrane affinities/activities of the studied peptaibols are discussed in relation to their hydrophobic and amphipathic properties.

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