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

2019Journal article Open access
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dc.contributor.authorVernen, Felicitas
dc.contributor.authorHarvey, Peta J.
dc.contributor.authorDias, Susana
dc.contributor.authorVeiga, Ana Salomé
dc.contributor.authorHuang, Yen-Hua
dc.contributor.authorCraik, David J.
dc.contributor.authorLawrence, Nicole
dc.contributor.authorTroeira Henriques, Sónia
dc.date.accessioned2021-10-15T14:19:55Z
dc.date.available2021-10-15T14:19:55Z
dc.date.issued2019
dc.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/).pt_PT
dc.description.abstractTachyplesin 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.pt_PT
dc.description.sponsorshipThis 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.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationInt J Mol Sci. 2019 Aug 26;20(17):4184.pt_PT
dc.identifier.doi10.3390/ijms20174184pt_PT
dc.identifier.eissn1422-0067
dc.identifier.issn1661-6596
dc.identifier.urihttp://hdl.handle.net/10451/49914
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationInnovative peptides against cancer and pathogenic bacteria, with advances in science, biopharmaceutical drug development, product market targeting, training , and communication.
dc.relation.publisherversionhttps://www.mdpi.com/journal/ijmspt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectAntibiofilmpt_PT
dc.subjectAnticancerpt_PT
dc.subjectAntimicrobialpt_PT
dc.subjectHost defense peptidept_PT
dc.subjectModel membranespt_PT
dc.subjectNuclear magnetic resonance solution structurept_PT
dc.subjectPeptide-membrane interactionpt_PT
dc.subjectStructure-activitypt_PT
dc.subjectTachyplesinpt_PT
dc.titleCharacterization of Tachyplesin peptides and their cyclized analogues to improve antimicrobial and anticancer propertiespt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleInnovative peptides against cancer and pathogenic bacteria, with advances in science, biopharmaceutical drug development, product market targeting, training , and communication.
oaire.awardURIinfo:eu-repo/grantAgreement/EC/H2020/644167/EU
oaire.citation.issue17pt_PT
oaire.citation.titleInternational Journal of Molecular Sciencespt_PT
oaire.citation.volume20pt_PT
oaire.fundingStreamH2020
person.familyNameDias
person.familyNameVeiga
person.givenNameSusana
person.givenNameAna Salome
person.identifier.ciencia-idF61D-0A28-659A
person.identifier.orcid0000-0001-8910-5404
person.identifier.orcid0000-0002-9892-2243
person.identifier.scopus-author-id56745037100
project.funder.identifierhttp://doi.org/10.13039/501100008530
project.funder.nameEuropean Commission
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication6b2869fd-0474-4f6c-bf5d-5973ee423da7
relation.isAuthorOfPublicatione4303354-5eaa-4d48-8198-de1adc9beb19
relation.isAuthorOfPublication.latestForDiscovery6b2869fd-0474-4f6c-bf5d-5973ee423da7
relation.isProjectOfPublicationde0ab284-92e7-489b-9316-562e1995a110
relation.isProjectOfPublication.latestForDiscoveryde0ab284-92e7-489b-9316-562e1995a110

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