6C41
The clavanin peptide in the presence of TFE (2,2,2-trifluoroethanol), presented a amphipathic alpha-helices from Phe-2 to Val-22 residues
Summary for 6C41
| Entry DOI | 10.2210/pdb6c41/pdb |
| NMR Information | BMRB: 30396 |
| Descriptor | Clavanin-A (1 entity in total) |
| Functional Keywords | antimicrobial peptides, biofilm, antimicrobial protein |
| Biological source | Styela clava (Sea squirt) |
| Total number of polymer chains | 1 |
| Total formula weight | 2670.12 |
| Authors | Alves, E.S.F.,Liao, L.M. (deposition date: 2018-01-11, release date: 2018-02-07, Last modification date: 2024-11-13) |
| Primary citation | Silva, O.N.,Alves, E.S.,de la Fuente-Nunez, C.,Ribeiro, S.M.,Mandal, S.M.,Gaspar, D.,Veiga, A.S.,Castanho, M.A.,Andrade, C.A.,Nascimento, J.M.,Fensterseifer, I.C.,Porto, W.F.,Correa, J.R.,Hancock, R.E.,Korpole, S.,Oliveira, A.L.,Liao, L.M.,Franco, O.L. Structural Studies of a Lipid-Binding Peptide from Tunicate Hemocytes with Anti-Biofilm Activity. Sci Rep, 6:27128-, 2016 Cited by PubMed 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. PubMed: 27292548DOI: 10.1038/srep27128 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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