دورية أكاديمية
A biophysical characterization of the interaction of a hepatitis C virus membranotropic peptide with micelles.
| العنوان: | A biophysical characterization of the interaction of a hepatitis C virus membranotropic peptide with micelles. |
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| المؤلفون: | Alves NS; Programa de Biologia Estrutural, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil; Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil., Mendes YS; Programa de Biologia Estrutural, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil; Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil., Souza TL; Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil; Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil., Bianconi ML; Programa de Biologia Estrutural, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil., Silva JL; Programa de Biologia Estrutural, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil; Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil., Gomes AM; Programa de Biologia Estrutural, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil; Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil. Electronic address: amog@bioqmed.ufrj.br., Oliveira AC; Programa de Biologia Estrutural, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil; Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil. Electronic address: cheble@bioqmed.ufrj.br. |
| المصدر: | Biochimica et biophysica acta [Biochim Biophys Acta] 2016 Apr; Vol. 1864 (4), pp. 359-71. Date of Electronic Publication: 2016 Jan 07. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Amsterdam : Elsevier Pub. Co. |
| مواضيع طبية MeSH: | Hepacivirus/*chemistry , Viral Envelope Proteins/*chemistry, Amino Acid Sequence ; Lipid Bilayers/chemistry ; Micelles ; Molecular Sequence Data ; Protein Structure, Secondary ; Spectrometry, Fluorescence ; Thermodynamics |
| مستخلص: | Membrane fusion is a highly regulated process that allows enveloped viruses to enter cells and replicate. Viral glycoproteins trigger membrane fusion by means of internal sequences known as fusion peptides. The hepatitis C virus (HCV) genome encodes the envelope glycoproteins E1 and E2, but their specific roles in the fusion step and the localization of the fusion peptide remain uncharacterized. Here, we studied the biophysics of the interactions between the glycoprotein E2 peptide HCV421-445 and four different micellar systems providing ionic, non-ionic and zwitterionic surfaces to investigate the importance of electrostatic interactions for peptide-membrane binding. Circular dichroism, fluorescence spectroscopy and calorimetry were used to characterize peptide-micelle interactions and structural changes. Fluorescence quenching showed that HCV421-445 interacts with SDS or CTAB ionic, n-OGP non-ionic and DPC zwitterionic micelles. The indole ring of Trp seems to anchor the peptide in micelles. Trp residues seem to be more deeply inserted in ionic and non-ionic micelles where peptide interactions are more stable than with DPC zwitterionic micelles. The interaction with zwitterionic micelles appears to occur at the surface. Both interaction types are exothermic because of peptide-micelle interactions and a gain of secondary structure in the helical conformation. HCV421-445 interacts with detergent monomers and micelles. Peptide-micelle interaction is pH-independent. HCV421-445 interacts with membranes, promoting aggregation and coalescence of vesicles with content leakage, suggesting that HCV421-445 may participate in membrane fusion. This structural characterization contributes to our understanding of the molecular process that promotes fusion, which is important in the further development of new antiviral therapies. (Copyright © 2016 Elsevier B.V. All rights reserved.) |
| فهرسة مساهمة: | Keywords: Hepacivirus; Hepatitis C virus; Peptide structure; Peptide–micelle interaction |
| المشرفين على المادة: | 0 (Lipid Bilayers) 0 (Micelles) 0 (Viral Envelope Proteins) |
| تواريخ الأحداث: | Date Created: 20160117 Date Completed: 20160519 Latest Revision: 20161126 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1016/j.bbapap.2016.01.003 |
| PMID: | 26773352 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0006-3002 |
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| DOI: | 10.1016/j.bbapap.2016.01.003 |