Advanced search
Start date
Betweenand
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

Full text
Author(s):
dos Santos Cabrera, Marcia Perez [1, 2] ; Arcisio-Miranda, Manoel [2] ; da Costa, Laiana Cristina [1] ; de Souza, Bibiana Monson [3] ; Broggio Costa, Sabrina Thais [1] ; Palma, Mario Sergio [3] ; Ruggiero Neto, Joao [1] ; Procopio, Joaquim [2]
Total Authors: 8
Affiliation:
[1] Sao Paulo State Univ, UNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[2] Univ Sao Paulo, Dept Physiol & Biophys, Inst Biomed Sci, Sao Paulo - Brazil
[3] Sao Paulo State Univ, UNESP, Ctr Studies Social Insects, Inst Biosci, Rio Claro, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Archives of Biochemistry and Biophysics; v. 486, n. 1, p. 1-11, JUN 1 2009.
Web of Science Citations: 21
Abstract

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 Inc. All rights reserved. (AU)

FAPESP's process: 06/57122-7 - Searching for lead compounds for rational development of new drugs and pesticides through bioprospecting in Brazilian arthropods
Grantee:Mario Sergio Palma
Support type: BIOTA-FAPESP Program - Thematic Grants