NDLI: Ion channels of various types induced in lipid membranes by gramicidin a derivatives carrying a cationic sequence at their C-termini

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Ion channels of various types induced in lipid membranes by gramicidin a derivatives carrying a cationic sequence at their C-termini

Content Provider	Springer Nature Link
Author	Stoilova, T. B. Dutseva, E. A. Pashkovskaya, A. A. Sychev, S. V. Koval’chuk, S. I. Sobko, A. A. Egorova, N. S. Kotova, E. A. Antonenko, Yu. N. Surovoi, A. Yu. Ivav, V. T.
Copyright Year	2007
Abstract	The channel-forming activity of gramicidin A derivatives carrying positively charged amino acid sequences at their C-termini was studied on planar bilayer lipid membranes and liposomes. We showed previously (FEBS Lett., 2005, vol. 579, pp. 5247–5252) that, at low concentrations, these peptides form classical cation-selective pores typical of gramicidin A, whereas, at high concentrations, they form large nonselective pores. The ability of the peptides to form nonselective pores, which was determined by the efflux of carboxyfluorescein, an organic dye, from liposomes, decreased substantially as the length of the gramicidin fragment in the series of cationic analogues was truncated. CD spectra showed that large pores are formed by peptides having both β$^{6.3}$ single-stranded and β$^{5.6}$ double-stranded helical conformations of the gramicidin fragment, with the C-terminal cationic sequence being extended. The dimerization of the peptides by the oxidation of the terminal cysteine promoted the formation of nonselective pores. It was shown that nonselective pores are not formed in membranes of erythrocytes, which may indicate a dependence of the channel-forming ability on the membrane type. The results may be of interest for the directed synthesis of peptides with antibacterial activity.
Starting Page	474
Ending Page	481
Page Count	8
File Format	PDF
ISSN	10681620
Journal	Russian Journal of Bioorganic Chemistry
Volume Number	33
Issue Number	5
e-ISSN	15739163
Language	English
Publisher	Nauka/Interperiodica
Publisher Date	2007-01-01
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	gramicidin, cationic analogues ion channels, nonselective pores transmembrane amphipathic peptides Biochemistry Bioorganic Chemistry Organic Chemistry Biomedicine general
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry

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