Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins
| Autor: | Jesús Salgado, Gianfranco Menestrina, Mauro Dalla Serra, Ismael Mingarro, M. Coraiola, Ana J. García-Sáez |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Molecular Sequence Data Biophysics Apoptosis Peptide In Vitro Techniques Biophysical Phenomena Ion Channels Permeability Protein Structure Secondary chemistry.chemical_compound Bcl-2-associated X protein Spectroscopy Fourier Transform Infrared Humans Channels Receptors and Electrical Signaling Amino Acid Sequence Peptide sequence Ion channel bcl-2-Associated X Protein chemistry.chemical_classification biology Chemistry Circular Dichroism Peptide Fragments Cell biology Calcein Membrane Proto-Oncogene Proteins c-bcl-2 Cytoplasm Multiprotein Complexes Liposomes biology.protein Pèptids Carrier Proteins Bacterial outer membrane Proteïnes BH3 Interacting Domain Death Agonist Protein |
| Zdroj: | García-Sáez, Ana Jesús Coraiola, Manuela Dalla Serra, Mauro Mingarro Muñoz, Ismael Menestrina, Gianfranco Salgado Benito, Jesús 2005 Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins Biophysical Journal 88 6 3976 3990 Biophysical journal 88 (2005): 3976–3990. doi:10.1529/biophysj.104.058008 info:cnr-pdr/source/autori:Ana J. Garcia-Saez;* Manuela Coraiola;y Mauro Dalla Serra;y Ismael Mingarro;* Gianfranco Menestrina;y and Jesus Salgado*/titolo:Peptides derived from apoptotic Bax and bid reproduce the poration activity of the parent full-length proteins./doi:10.1529%2Fbiophysj.104.058008/rivista:Biophysical journal (Print)/anno:2005/pagina_da:3976/pagina_a:3990/intervallo_pagine:3976–3990/volume:88 RODERIC. Repositorio Institucional de la Universitat de Valéncia instname |
| ISSN: | 0006-3495 |
| Popis: | Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they form ion conducting channels, which in the case of the Bax-derived peptide are characterized by a two-stage pattern, a large conductivity and lipid-charge-dependent ionic selectivity. These features, together with the influence of intrinsic lipid curvature on the poration activity and the existence of two helical stretches of different orientations for the membrane-bound peptide, suggest that it forms mixed lipidic/peptidic pores of toroidal structure. In contrast, the assayed Bid fragment shows a markedly different behavior, characterized by the formation of discrete, steplike channels in planar lipid bilayers, as expected for a peptidic pore lined by a bundle of helices. |
| Databáze: | OpenAIRE |
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