Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca

Abstract Palustrin-Ca (GFLDIIKDTGKEFAVKILNNLKCKLAGGCPP) is a host defence peptide with potent antimicrobial and anticancer activities, first isolated from the skin of the American bullfrog Lithobates catesbeianus. The peptide is 31 amino acid residues long, cationic and amphipathic. Two-dimensional...

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Autores principales:	Patrick B. Timmons, Chandralal M. Hewage
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c3dab677778d40a28439e7348ceca70e
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spelling	oai:doaj.org-article:c3dab677778d40a28439e7348ceca70e2021-11-21T12:20:55ZConformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca10.1038/s41598-021-01769-32045-2322https://doaj.org/article/c3dab677778d40a28439e7348ceca70e2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-01769-3https://doaj.org/toc/2045-2322Abstract Palustrin-Ca (GFLDIIKDTGKEFAVKILNNLKCKLAGGCPP) is a host defence peptide with potent antimicrobial and anticancer activities, first isolated from the skin of the American bullfrog Lithobates catesbeianus. The peptide is 31 amino acid residues long, cationic and amphipathic. Two-dimensional NMR spectroscopy was employed to characterise its three-dimensional structure in a 50/50% water/2,2,2-trifluoroethanol- $$d_{3}$$ d 3 mixture. The structure is defined by an $$\alpha$$ α -helix that spans between Ile $$^{6}$$ 6 -Ala $$^{26}$$ 26 , and a cyclic disulfide-bridged domain at the C-terminal end of the peptide sequence, between residues 23 and 29. A molecular dynamics simulation was employed to model the peptide’s interactions with sodium dodecyl sulfate micelles, a widely used bacterial membrane-mimicking environment. Throughout the simulation, the peptide was found to maintain its $$\alpha$$ α -helical conformation between residues Ile $$^{6}$$ 6 -Ala $$^{26}$$ 26 , while adopting a position parallel to the surface to micelle, which is energetically-favourable due to many hydrophobic and electrostatic contacts with the micelle.Patrick B. TimmonsChandralal M. HewageNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Patrick B. Timmons Chandralal M. Hewage Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca
description	Abstract Palustrin-Ca (GFLDIIKDTGKEFAVKILNNLKCKLAGGCPP) is a host defence peptide with potent antimicrobial and anticancer activities, first isolated from the skin of the American bullfrog Lithobates catesbeianus. The peptide is 31 amino acid residues long, cationic and amphipathic. Two-dimensional NMR spectroscopy was employed to characterise its three-dimensional structure in a 50/50% water/2,2,2-trifluoroethanol- $$d_{3}$$ d 3 mixture. The structure is defined by an $$\alpha$$ α -helix that spans between Ile $$^{6}$$ 6 -Ala $$^{26}$$ 26 , and a cyclic disulfide-bridged domain at the C-terminal end of the peptide sequence, between residues 23 and 29. A molecular dynamics simulation was employed to model the peptide’s interactions with sodium dodecyl sulfate micelles, a widely used bacterial membrane-mimicking environment. Throughout the simulation, the peptide was found to maintain its $$\alpha$$ α -helical conformation between residues Ile $$^{6}$$ 6 -Ala $$^{26}$$ 26 , while adopting a position parallel to the surface to micelle, which is energetically-favourable due to many hydrophobic and electrostatic contacts with the micelle.
format	article
author	Patrick B. Timmons Chandralal M. Hewage
author_facet	Patrick B. Timmons Chandralal M. Hewage
author_sort	Patrick B. Timmons
title	Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca
title_short	Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca
title_full	Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca
title_fullStr	Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca
title_full_unstemmed	Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca
title_sort	conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-ca
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c3dab677778d40a28439e7348ceca70e
work_keys_str_mv	AT patrickbtimmons conformationandmembraneinteractionstudiesofthepotentantimicrobialandanticancerpeptidepalustrinca AT chandralalmhewage conformationandmembraneinteractionstudiesofthepotentantimicrobialandanticancerpeptidepalustrinca
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Conformation and membrane interaction studies of the potent antimicrobial and anticancer peptide palustrin-Ca

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