Structural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activity

Osmar N. Silva, Eliane S.F. Alves, César De La Fuente-Nñez, 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 Hancock, Suresh Korpole, Aline L. Oliveira, Luciano M. Liao, Octavio L. Franco

Research output: Contribution to journalArticle

12 Citations (Scopus)

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-d 3 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.

LanguageEnglish
Article number27128
JournalScientific Reports
Volume6
DOIs
Publication statusPublished - 13 Jun 2016
Externally publishedYes

ASJC Scopus subject areas

  • General

Cite this

Silva, O. N., Alves, E. S. F., De La Fuente-Nñez, C., Ribeiro, S. M., Mandal, S. M., Gaspar, D., ... Franco, O. L. (2016). Structural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activity. Scientific Reports, 6, [27128]. https://doi.org/10.1038/srep27128
Silva, Osmar N. ; Alves, Eliane S.F. ; De La Fuente-Nñez, César ; Ribeiro, Suzana M. ; Mandal, Santi M. ; Gaspar, Diana ; Veiga, Ana S. ; Castanho, Miguel A.R.B. ; Andrade, Cesar A.S. ; Nascimento, Jessica M. ; Fensterseifer, Isabel C.M. ; Porto, William F. ; Correa, Jose R. ; Hancock, Robert ; Korpole, Suresh ; Oliveira, Aline L. ; Liao, Luciano M. ; Franco, Octavio L. / Structural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activity. In: Scientific Reports. 2016 ; Vol. 6.
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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-d 3 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.",
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Silva, ON, Alves, ESF, De La Fuente-Nñez, C, Ribeiro, SM, Mandal, SM, Gaspar, D, Veiga, AS, Castanho, MARB, Andrade, CAS, Nascimento, JM, Fensterseifer, ICM, Porto, WF, Correa, JR, Hancock, R, Korpole, S, Oliveira, AL, Liao, LM & Franco, OL 2016, 'Structural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activity', Scientific Reports, vol. 6, 27128. https://doi.org/10.1038/srep27128

Structural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activity. / Silva, Osmar N.; Alves, Eliane S.F.; De La Fuente-Nñez, César; Ribeiro, Suzana M.; Mandal, Santi M.; Gaspar, Diana; Veiga, Ana S.; Castanho, Miguel A.R.B.; Andrade, Cesar A.S.; Nascimento, Jessica M.; Fensterseifer, Isabel C.M.; Porto, William F.; Correa, Jose R.; Hancock, Robert; Korpole, Suresh; Oliveira, Aline L.; Liao, Luciano M.; Franco, Octavio L.

In: Scientific Reports, Vol. 6, 27128, 13.06.2016.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Structural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activity

AU - Silva, Osmar N.

AU - Alves, Eliane S.F.

AU - De La Fuente-Nñez, César

AU - Ribeiro, Suzana M.

AU - Mandal, Santi M.

AU - Gaspar, Diana

AU - Veiga, Ana S.

AU - Castanho, Miguel A.R.B.

AU - Andrade, Cesar A.S.

AU - Nascimento, Jessica M.

AU - Fensterseifer, Isabel C.M.

AU - Porto, William F.

AU - Correa, Jose R.

AU - Hancock, Robert

AU - Korpole, Suresh

AU - Oliveira, Aline L.

AU - Liao, Luciano M.

AU - Franco, Octavio L.

PY - 2016/6/13

Y1 - 2016/6/13

N2 - 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-d 3 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.

AB - 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-d 3 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.

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U2 - 10.1038/srep27128

DO - 10.1038/srep27128

M3 - Article

VL - 6

JO - Scientific Reports

T2 - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 27128

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Silva ON, Alves ESF, De La Fuente-Nñez C, Ribeiro SM, Mandal SM, Gaspar D et al. Structural studies of a lipid-binding peptide from tunicate hemocytes with anti-biofilm activity. Scientific Reports. 2016 Jun 13;6. 27128. https://doi.org/10.1038/srep27128