Structural Studies of a Lipid-Binding Peptide from Tunicate Hemocytes with Anti-Biofilm Activity View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-07

AUTHORS

Osmar N Silva, Eliane S F Alves, César de la Fuente-Núñez, Suzana M Ribeiro, Santi M Mandal, Diana Gaspar, Ana S Veiga, Miguel A R B Castanho, Cesar A S Andrade, Jessica M Nascimento, Isabel C M Fensterseifer, William F Porto, Jose R Correa, Robert E W Hancock, Suresh Korpole, Aline L Oliveira, Luciano M Liao, Octavio L Franco

ABSTRACT

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. More... »

PAGES

27128

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep27128

DOI

http://dx.doi.org/10.1038/srep27128

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1024105358

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27292548


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450 schema:name Department of Cellular Biology, Institute of Biological Sciences, University of Brasilia, Brasilia, 70910900, Brazil.
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455 schema:name Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon, Portugal.
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