Peculiarities of lytic action of melittin and its analog [Ala-14] melittin
Keywords:
melittin, [Ala-14]melittin, erythrocyte, hemolysis, divalent cations, chlorpromazine
Abstract
It is shown that lytic peptides melittin (M), melittin analog [Ala-14]melittin (P14A), and whole bee venom act in a different manner relative to human red blood cells (RBC). The normalized rate of hemolysis depended linearly on the relative amount of P14A in the mixture with both melittin and bee venom. The dose-response curve for P14A showed saturation only when the lytic effect of membrane-bound melittin was inhibited by chlorpromazine. This indicates that melittin and P14A produce hemolysis acting independently on each other. In contrast to melittin, but similar to bee venom, P14A also reduced the volume of lysed cells. Non-linear effects of cells shrinkage induced by mixtures of P14A with melittin and bee venom suggest that synergistic action of peptide analogs underlies the mechanism of this phenomenon. In addition, data suggest that melittin and P14A produce lytic effects through binding to different classes of sites on the RBC membrane. We conclude that the structure of lytic peptide is a predominant factor which in concert with the mode of peptide-membrane interactions modulates its lytic power.
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References
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Raghuraman H, Chattopadhvay A. Cholesterol inhibits the lytic activity of melittin in erythrocytes. Chem Phys Lipids. 2005;134(2):183-9.
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Portlock SH, Clague MJ, Cherry RJ. Leakage of internal markers from erythrocytes and lipid vesicles induced by melittin, gramicidin S and alamethicin: a comparative study. Biochim. Biophys. Acta. 1990;1030:1-10.
Subbarao NK, MacDonald RC. Lipid unsaturation influences melittin-induced leakage of vesicles. Biochim. Biophys. Acta. 1994;1189:101-7.
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Alder GM, Arnold WM, Bashford CL. Divalent cation-sensitive pores formed by natural and synthetic melittin and by triron X-100. Biochim. Biophys. Acta. 1991;1061:111-20.
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Dempsey C, Sternberg B. Reversible disc-micellization of dimyristoylphosphatidylcholine bilayers induced by melittin and [Ala-14] melittin. Biochim. Biophys. Acta. 1991;1061:175-84.
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Cornut I, Buttner K, Dasseux JL, Dufourcq J. The amphipathic alpha-helix concept. Application to the de novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin. FEBS. Lett. 1994;349:29-33.
Asthana N, Yadav SP, Ghosh JK. Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role determining its hemolytic activity but not antibacterial activity. J. Biol. Chem. 2004;279:55042-50.
Yan H, Li S, Sun X. Individual substitution analogs of Mel(12-26), melittin's C-terminal 15-residue peptide: their antimicrobial and hemolvtic action. FEBS Lett. 2003;554:100-4.
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Subbalakshmi C, Nagaraj R, Sitaram N. Biological activities of C-terminal 15-residue synthetic fragment of melittin: design of an analog with improved antibacterial activity. FEBS Lett. 1999;448:62-6.
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Richiery GV, Mel HC. Membrane and cytoplasmic resistivity properties of normal and sickle red blood cells. Cell Biophysical. 1986;8:243-59.
Tosteson MT, Holmes SJ, Rasin M, Tosteson DC. Melittin lysis of red cells. J. Membr. Biol. 1985;87:35-44.
Tanaka Y, Mashino K, Inoue K, Nojima S. Mechanism of human erythrocyte hemolysis induced by short-chain phosphatidylcholines and lysophosphatidycholine. J. Biochem. 1983;94:833-40.
Tang GQ, Iida T, Yamamoto K, Honda T. A mutant toxin of vibrio parahaemolyticus thermostable direct hemolysin which has lost hemolytic activity but retains ability to bind to erythrocytes. Infect. Immun. 1994;62:3299-304.
Rudenko SV, Bojok GA, Nipot EE. Bee venom-induced shrinkage of erythrocyte ghosts. Biochemistry (Moscow). 1997;62:104-9.
Fattal E, Nir S, Parente RA, Szoka FC. Pore-forming peptides induce rapid phospholipid flip-flop in membranes. Biochemistry.1994;33:6721-31.
Svoboda K, Schmidt CF, Branton D, Block SM. Conformation and elasticity of the isolated red blood cell membrane skeleton. Biophys. J. 1992;63:784-93.
Vertssy BG, Steck TL. Elasticity of the human red cell membrane skeleton. Effect of temperature and denaturants. Biophys. J. 1989;55:255-62.
Bashford CL, Alder GM, Graham. Ion modulation of membrane permeability: effect of cations on intact cells and on cells and phospholipid bilayers treated with pore-forming agents. J. Memmbrane Biol. 1988;103:79-94.
Dempsey CE. The action of melittin on membranes. Biochim. Biophys. Acta. 1990;1031:143-61.
Raghuraman H, Chattopadhvay A. Cholesterol inhibits the lytic activity of melittin in erythrocytes. Chem Phys Lipids. 2005;134(2):183-9.
Mahaney JE, Kleinschmindt J, Marsh D, Thomas DD. Effect of melittin on lipid-protein interaction in sarcoplasmic reticulum membranes. Biophys. J. 1992;63:1513-22.
Portlock SH, Clague MJ, Cherry RJ. Leakage of internal markers from erythrocytes and lipid vesicles induced by melittin, gramicidin S and alamethicin: a comparative study. Biochim. Biophys. Acta. 1990;1030:1-10.
Subbarao NK, MacDonald RC. Lipid unsaturation influences melittin-induced leakage of vesicles. Biochim. Biophys. Acta. 1994;1189:101-7.
Van Veen M, Cherry RJ. The effect of integral membrane protein (human band 3) on the membrane lytic properties of melittin in reconstituted systems, FEMS Microbiol. Immunol. 1992;105:147-50.
Alder GM, Arnold WM, Bashford CL. Divalent cation-sensitive pores formed by natural and synthetic melittin and by triron X-100. Biochim. Biophys. Acta. 1991;1061:111-20.
Rudenko SV, Nipot EE. Protection by chlorpromazine, albumin and divalent cations of hemolysis induced by melittin, [ala-14] melittin and whole bee venom. Biochem. J. 1994;317(3):747-54.
Rudenko SV, Nipot EE. Modulation of melittin- induced hemolysis of Red Blood Cells. Biochemistry (Moscow) 1996;61:1524-31.
De Grado WF, Musso GF, Lieber M. Kinetics and mechanism of hemolysis induced by melittin and by a syntheie melittin analogue. Biophys. J.1982;37:329-38.
Dempsey C, Sternberg B. Reversible disc-micellization of dimyristoylphosphatidylcholine bilayers induced by melittin and [Ala-14] melittin. Biochim. Biophys. Acta. 1991;1061:175-84.
Dempsey C, Bazzo R, Harvey TS. Contribution of proline – 14 to the structure and action of melittin. FEBS Lett. 1991;281:240-4.
Cornut I, Buttner K, Dasseux JL, Dufourcq J. The amphipathic alpha-helix concept. Application to the de novo design of ideally amphipathic Leu, Lys peptides with hemolytic activity higher than that of melittin. FEBS. Lett. 1994;349:29-33.
Asthana N, Yadav SP, Ghosh JK. Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role determining its hemolytic activity but not antibacterial activity. J. Biol. Chem. 2004;279:55042-50.
Yan H, Li S, Sun X. Individual substitution analogs of Mel(12-26), melittin's C-terminal 15-residue peptide: their antimicrobial and hemolvtic action. FEBS Lett. 2003;554:100-4.
Hewish DR, Barnham KJ, Werkmeister JA. Structure and activity of D-Pro14 melittin. J. Protein Chem. 2002;21:243-53.
Unger T, Oren Z, Shai Y. The effect of cyclization of magainin 2 and melittin analogues on structure, function, and model membrane interactions: implication to their mode of action. Biochemistry. 2001;40:6388-97.
Subbalakshmi C, Nagaraj R, Sitaram N. Biological activities of C-terminal 15-residue synthetic fragment of melittin: design of an analog with improved antibacterial activity. FEBS Lett. 1999;448:62-6.
Shin SY, Kang JH, Hahm KS. Structure-antibacterial, antitumor and hemolytic activity relationships of cecropin A-magainin 2 and cecropin A-melittin hybrid peptides. J. Pept. Res. 1999;53:82-90.
Oren Z, Shai Y. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry. 1997;36:1826-35.
Habermann E. Bee and Wasp venom. Science. 1972;177:314-22.
Akeson SP, Mel HC. Deformability and other rheological interactions of red blood cells in electronic cell sizing. Biorheology. 1986;23:1-15.
Richiery GV, Mel HC. Membrane and cytoplasmic resistivity properties of normal and sickle red blood cells. Cell Biophysical. 1986;8:243-59.
Tosteson MT, Holmes SJ, Rasin M, Tosteson DC. Melittin lysis of red cells. J. Membr. Biol. 1985;87:35-44.
Tanaka Y, Mashino K, Inoue K, Nojima S. Mechanism of human erythrocyte hemolysis induced by short-chain phosphatidylcholines and lysophosphatidycholine. J. Biochem. 1983;94:833-40.
Tang GQ, Iida T, Yamamoto K, Honda T. A mutant toxin of vibrio parahaemolyticus thermostable direct hemolysin which has lost hemolytic activity but retains ability to bind to erythrocytes. Infect. Immun. 1994;62:3299-304.
Rudenko SV, Bojok GA, Nipot EE. Bee venom-induced shrinkage of erythrocyte ghosts. Biochemistry (Moscow). 1997;62:104-9.
Fattal E, Nir S, Parente RA, Szoka FC. Pore-forming peptides induce rapid phospholipid flip-flop in membranes. Biochemistry.1994;33:6721-31.
Svoboda K, Schmidt CF, Branton D, Block SM. Conformation and elasticity of the isolated red blood cell membrane skeleton. Biophys. J. 1992;63:784-93.
Vertssy BG, Steck TL. Elasticity of the human red cell membrane skeleton. Effect of temperature and denaturants. Biophys. J. 1989;55:255-62.
Published
2005-06-06
Cited
How to Cite
Rudenko, S. V., & Madanat, W. K. J. (2005). Peculiarities of lytic action of melittin and its analog [Ala-14] melittin. Biophysical Bulletin, 2(16), 47-52. Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/13417
Section
Cell biophysics
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