Evidence map›Paper›PMID 31455019›Full record

ArticleInternational journal of molecular sciences2019

Characterization of Tachyplesin Peptides and Their Cyclized Analogues to Improve Antimicrobial and Anticancer Properties.

Felicitas Vernen, Peta J Harvey, Susana A Dias, Ana Salomé Veiga, Yen-Hua Huang, David J Craik, Nicole Lawrence, Sónia Troeira Henriques

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed.

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  18. Review
  19. Efficient Mining of Anticancer Peptides from Gut Metagenome.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  20. Going Beyond Host Defence Peptides: Horizons of Chemically Engineered Peptides for Multidrug-Resistant Bacteria.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Felicitas VernenInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0001-6658-0376
Peta J HarveyInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0003-4735-6242
Susana A DiasInstituto de Medicina Molecular João Lobo Antunes, Faculdade de Medicina, Universidade de Lisboa, 1649-028 Lisboa, Portugal.ORCID 0000-0001-8910-5404
Ana Salomé VeigaInstituto de Medicina Molecular João Lobo Antunes, Faculdade de Medicina, Universidade de Lisboa, 1649-028 Lisboa, Portugal.ORCID 0000-0002-9892-2243
Yen-Hua HuangInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0001-6937-2660
David J CraikInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0003-0007-6796
Nicole LawrenceInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0002-9013-1770
Sónia Troeira HenriquesInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Queensland 4072, Australia. sonia.henriques@qut.edu.au.ORCID 0000-0001-9564-9651

Funding

Australian Research Council FL150100146Australian Research Council FT150100398Marie Skłodowska-Curie Research and Innovation Staff Exchange 644167National Health and Medical Research Council APP1084965
6 · The paper itself

Abstract

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.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntineoplastic AgentsCell Line, TumorCyclizationDNA-Binding ProteinsDrug StabilityHumansMicrobial Sensitivity TestsMolecular ConformationMolecular StructurePeptides, CyclicSpectrometry, FluorescenceStructure-Activity RelationshipAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntineoplastic AgentsDNA-Binding ProteinsPeptides, Cyclictachyplesin peptide, Tachypleus tridentatusantibiofilmanticancerantimicrobialhost defense peptidemodel membranesnuclear magnetic resonance solution structurepeptide-membrane interactionstructure-activitytachyplesin

Identifiers

PMID31455019
PMCPMC6747087

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.