Structural Studies of a Lipid-Binding Peptide from Tunicate Hemocytes with Anti-Biofilm Activity
| Autor: | Diana Gaspar, Santi M. Mandal, William F. Porto, Osmar N. Silva, Suzana M. Ribeiro, Isabel C. M. Fensterseifer, Eliane S. F. Alves, Cesar de la Fuente-Nunez, Jéssica M. Nascimento, Octavio L. Franco, César Andrade, Luciano M. Lião, Miguel A. R. B. Castanho, Aline L. de Oliveira, José R. Corrêa, Robert E. W. Hancock, Suresh Korpole, Ana Salomé Veiga |
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| Přispěvatelé: | Repositório da Universidade de Lisboa |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Circular dichroism Hemocytes 030106 microbiology Lipid Bilayers ComputingMilieux_LEGALASPECTSOFCOMPUTING Peptide Microbial Sensitivity Tests Biology Bacterial Physiological Phenomena Article Protein Structure Secondary Cell membrane 03 medical and health sciences chemistry.chemical_compound medicine Animals Urochordata Sodium dodecyl sulfate Lipid bilayer chemistry.chemical_classification Multidisciplinary Bacteria Circular Dichroism Cell Membrane Biofilm Blood Proteins Dynamic Light Scattering 3. Good health Molecular Docking Simulation 030104 developmental biology Membrane medicine.anatomical_structure chemistry Biochemistry Docking (molecular) Data_GENERAL Biofilms |
| Zdroj: | Scientific Reports Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| ISSN: | 2045-2322 |
| Popis: | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ Clavanins is a class of peptides (23aa) histidine-rich, free of post-translational modifications. Clavanins have been studied largely for their ability to disrupt bacterial membranes. In the present study, the interaction of clavanin A with membranes was assessed by dynamic light scattering, zeta potential and permeabilization assays. We observed through those assays that clavanin A lysis bacterial cells at concentrations corresponding to its MIC. Further, the structure and function of clavanin A was investigated. To better understand how clavanin interacted with bacteria, its NMR structure was elucidated. The solution state NMR structure of clavanin A in the presence of TFE-d3 indicated an α-helical conformation. Secondary structures, based on circular dichroism measurements in anionic sodium dodecyl sulfate (SDS) and TFE (2,2,2-trifluorethanol), in silico lipid-peptide docking and molecular simulations with lipids DPPC and DOPC revealed that clavanin A can adopt a variety of folds, possibly influencing its different functions. Microcalorimetry assays revealed that clavanin A was capable of discriminating between different lipids. Finally, clavanin A was found to eradicate bacterial biofilms representing a previously unrecognized function. We would like to thank CNPq, CAPES (Ciências sem Fronteiras), FAPDF and FUNDECT. D.G. acknowledges Fundação para a Ciência e a Tecnologia - Ministério da Educação e Ciência (FCT-MEC, Portugal) for fellowship SFRH/BPD/73500/2010 and A.S.V. for funding within the FCT Investigator Programme (IF/00803/2012). |
| Databáze: | OpenAIRE |
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