Interactions of mast cell degranulating peptides with model membranes: A comparative biophysical study

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dos Santos Cabrera, Marcia Perez [UNESP]
Arcisio-Miranda, Manoel
da Costa, Laiana Cristina [UNESP]
de Souza, Bibiana Monson [UNESP]
Broggio Costa, Sabrina Thais [UNESP]
Palma, Mario Sergio [UNESP]
Ruggiero Neto, Joao [UNESP]
Procopio, Joaquim

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Elsevier B.V.


In the last decade, there has been renewed interest in biologically active peptides in fields like allergy, autoimmume diseases and antibiotic therapy. Mast cell degranulating peptides mimic G-protein receptors, showing different activity levels even among homologous peptides. Another important feature is their ability to interact directly with membrane phospholipids, in a fast and concentration-dependent way. The mechanism of action of peptide HR1 on model membranes was investigated comparatively to other mast cell degranulating peptides (Mastoparan, Eumenitin and Anoplin) to evidence the features that modulate their selectivity. Using vesicle leakage, single-channel recordings and zeta-potential measurements, we demonstrated that HR1 preferentially binds to anionic bilayers, accumulates, folds, and at very low concentrations, is able to insert and create membrane spanning ion-selective pores. We discuss the ion selectivity character of the pores based on the neutralization or screening of the peptides charges by the bilayer head group charges or dipoles. (C) 2009 Elsevier B.V. All rights reserved.



Mastoparan peptide HR1, Anoplin, Eumenitin, Peptide-membrane interaction, Ion channel-like activity, Mast cell degranulating peptides, Lytic activity, Ionic selectivity, Pore activity, Zeta-potential

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Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 486, n. 1, p. 1-11, 2009.