Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties

Detalhes bibliográficos
Autor(a) principal: Vernen, Felicitas
Data de Publicação: 2019
Outros Autores: Harvey, Peta J., Dias, Susana, Veiga, Ana Salomé, Huang, Yen-Hua, Craik, David J., Lawrence, Nicole, Troeira Henriques, Sónia
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/49914
Resumo: © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
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spelling Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer propertiesAntibiofilmAnticancerAntimicrobialHost defense peptideModel membranesNuclear magnetic resonance solution structurePeptide-membrane interactionStructure-activityTachyplesin© 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).Tachyplesin I, II and III are host defense peptides from horseshoe crab species with antimicrobial and anticancer activities. They have an amphipathic β-hairpin structure, are highly positively-charged and differ by only one or two amino acid residues. In this study, we compared the structure and activity of the three tachyplesin peptides alongside their backbone cyclized analogues. We assessed the peptide structures using nuclear magnetic resonance (NMR) spectroscopy, then compared the activity against bacteria (both in the planktonic and biofilm forms) and a panel of cancerous cells. The importance of peptide-lipid interactions was examined using surface plasmon resonance and fluorescence spectroscopy methodologies. Our studies showed that tachyplesin peptides and their cyclic analogues were most potent against Gram-negative bacteria and melanoma cell lines, and showed a preference for binding to negatively-charged lipid membranes. Backbone cyclization did not improve potency, but improved peptide stability in human serum and reduced toxicity toward human red blood cells. Peptide-lipid binding affinity, orientation within the membrane, and ability to disrupt lipid bilayers differed between the cyclized peptide and the parent counterpart. We show that tachyplesin peptides and cyclized analogues have similarly potent antimicrobial and anticancer properties, but that backbone cyclization improves their stability and therapeutic potential.This project was funded by a National Health Medical Research Council (NHMRC) project grant (APP1084965). F.V. was supported by the UQ Research Scholarship, S.T.H. is an Australian Research Council (ARC) Future Fellow (FT150100398), D.J.C. is an ARC Australian Laureate Fellow (FL150100146). Marie Skłodowska-Curie Research and Innovation Staff Exchange grant (RISE; call: H2020-MSCA-RISE-2014, grant agreement 644167) funded secondments of S.A.D. and of A.S.V. to the University of Queensland. The Translational Research Institute is supported by a grant from the Australian Government.MDPIRepositório da Universidade de LisboaVernen, FelicitasHarvey, Peta J.Dias, SusanaVeiga, Ana SaloméHuang, Yen-HuaCraik, David J.Lawrence, NicoleTroeira Henriques, Sónia2021-10-15T14:19:55Z20192019-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/49914engInt J Mol Sci. 2019 Aug 26;20(17):4184.1661-659610.3390/ijms201741841422-0067info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T16:53:53Zoai:repositorio.ul.pt:10451/49914Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T22:01:26.437254Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties
title Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties
spellingShingle Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties
Vernen, Felicitas
Antibiofilm
Anticancer
Antimicrobial
Host defense peptide
Model membranes
Nuclear magnetic resonance solution structure
Peptide-membrane interaction
Structure-activity
Tachyplesin
title_short Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties
title_full Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties
title_fullStr Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties
title_full_unstemmed Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties
title_sort Characterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer properties
author Vernen, Felicitas
author_facet Vernen, Felicitas
Harvey, Peta J.
Dias, Susana
Veiga, Ana Salomé
Huang, Yen-Hua
Craik, David J.
Lawrence, Nicole
Troeira Henriques, Sónia
author_role author
author2 Harvey, Peta J.
Dias, Susana
Veiga, Ana Salomé
Huang, Yen-Hua
Craik, David J.
Lawrence, Nicole
Troeira Henriques, Sónia
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Vernen, Felicitas
Harvey, Peta J.
Dias, Susana
Veiga, Ana Salomé
Huang, Yen-Hua
Craik, David J.
Lawrence, Nicole
Troeira Henriques, Sónia
dc.subject.por.fl_str_mv Antibiofilm
Anticancer
Antimicrobial
Host defense peptide
Model membranes
Nuclear magnetic resonance solution structure
Peptide-membrane interaction
Structure-activity
Tachyplesin
topic Antibiofilm
Anticancer
Antimicrobial
Host defense peptide
Model membranes
Nuclear magnetic resonance solution structure
Peptide-membrane interaction
Structure-activity
Tachyplesin
description © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-01-01T00:00:00Z
2021-10-15T14:19:55Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10451/49914
url http://hdl.handle.net/10451/49914
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Int J Mol Sci. 2019 Aug 26;20(17):4184.
1661-6596
10.3390/ijms20174184
1422-0067
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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