Evidence map›Paper›PMID 39571778›Full record

ArticleExperimental eye research2025

The effect of immobilisation strategies on the ability of peptoids to reduce the adhesion of P. aeruginosa strains to contact lenses.

Manjulatha Sara, Sudip Chakraborty, Renxun Chen, Dennis Palms, Georgio Katsifis, Zhongyan Li, Syamak Farajikhah, Vinod Massedupally, Alex Hui, Edgar H H Wong and 10 more

Abstract read
In one paragraph

Article in Experimental eye research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Antimicrobial activity of a short guanidine mimic immobilised on contact lenses.Journal of materials science. Materials in medicine · 2026
    Article
  5. International journal of molecular sciences · 2025
    Review
  6. 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

20 authors.

Manjulatha SaraSchool of Optometry and Vision Science, UNSW Sydney, Australia. Electronic address: Manjulatha.sara@unsw.edu.au.
Sudip ChakrabortySchool of Chemistry, UNSW Sydney, Australia. Electronic address: s.chakraborty@unsw.edu.au.
Renxun ChenSchool of Chemistry, UNSW Sydney, Australia. Electronic address: r.chen@unsw.edu.au.
Dennis PalmsBiomedical Nanoengineering Laboratory, College of Medicine and Public Health, Flinders University, Bedford Park, SA, 5042, Australia. Electronic address: dennis.palms@flinders.edu.au.
Georgio KatsifisSchool of Physics, University of Sydney, NSW, 2006, Australia. Electronic address: gkat2146@uni.sydney.edu.au.
Zhongyan LiUniversity of Sydney, Australia. Electronic address: zhongyan.li@sydney.edu.au.
Syamak FarajikhahSchool of Chemical Engineering, UNSW Sydney, Australia. Electronic address: syamak.farajikhah@sydney.edu.au.
Vinod MassedupallySchool of Optometry and Vision Science, UNSW Sydney, Australia. Electronic address: vinodm@unsw.edu.au.
Alex HuiSchool of Optometry and Vision Science, UNSW Sydney, Australia; Centre for Ocular Research and Education, University of Waterloo, Canada. Electronic address: alex.hui@unsw.edu.au.
Edgar H H WongSchool of Optometry and Vision Science, UNSW Sydney, Australia; School of Chemical Engineering, UNSW Sydney, Australia. Electronic address: edgar.wong@unsw.edu.au.
Naresh KumarSchool of Chemistry, UNSW Sydney, Australia. Electronic address: n.kumar@unsw.edu.au.
Krasimir VasilevBiomedical Nanoengineering Laboratory, College of Medicine and Public Health, Flinders University, Bedford Park, SA, 5042, Australia. Electronic address: krasimir.vasilev@flinders.edu.au.
David MackenzieSchool of Physics, University of Sydney, NSW, 2006, Australia. Electronic address: david.mckenzie@sydney.edu.au.
Linda LosurdoSchool of Physics, University of Sydney, NSW, 2006, Australia. Electronic address: linda.losurdo@sydney.edu.au.
Farida DehghaniUniversity of Sydney, Australia. Electronic address: fariba.dehghani@sydney.edu.au.
Havard JenssenDepartment of Science and Environment, Roskilde University, 4000, Roskilde, Denmark. Electronic address: jenssen@ruc.dk.
Kristian SorensenDepartment of Bioengineering, School of Medicine & School of Engineering, Standford University, California, 94305, USA. Electronic address: ksoren@stanford.edu.
Jennifer S LinDepartment of Bioengineering, School of Medicine & School of Engineering, Standford University, California, 94305, USA. Electronic address: jlin3@stanford.edu.
Annelise E BarronDepartment of Bioengineering, School of Medicine & School of Engineering, Standford University, California, 94305, USA. Electronic address: aebarron@stanford.edu.
Mark WillcoxSchool of Optometry and Vision Science, UNSW Sydney, Australia. Electronic address: m.willcox@unsw.edu.au.

Funding

Role of Innate Immune Dysregulation in the Etiology of DementiaDP1AG072438 · NIA · STANFORD UNIVERSITY · PI BARRON, ANNELISE EMILY · 2020 to 2024
$5.2M
NIA NIH HHS DP1 AG072438
6 · The paper itself

Abstract

aimPrevious studies have demonstrated that contact lenses coated with the antimicrobial cationic peptide Mel4, a derivative of melimine, can reduce the occurrence of keratitis. However, the antimicrobial activity of Mel4 weakened over time due to its susceptibility to proteolytic degradation. Oligo-N-substituted glycine peptoids such as TM5 and TM18 possess antimicrobial properties and are resistant to proteolytic breakdown. This study focused on exploring methods for covalently attaching these peptoids to contact lenses to enhance their durability and performance in vitro.

methodsThe peptoids TM5 and TM18 were covalently attached to etafilcon lenses via carbodiimide chemistry (EDC/NHS), oxazoline plasma, and plasma ion immersion implantation (PIII). The lenses were analysed using X-ray photoelectron spectroscopy (XPS), surface charge, and hydrophobicity. Inhibition of adhesion of multidrug-resistant Pseudomonas aeruginosa and cytotoxicity on corneal epithelial cells were evaluated. The impact of moist heat sterilization on activity was also assessed.

resultsXPS confirmed peptoid binding to lenses. Peptoid coatings slightly increased contact angles (≤23°) without affecting overall charge. Peptoids, bound via carbodiimide, inhibited P. aeruginosa adhesion by over 5 log10 CFU per lens, outperforming melimine, which required six times the concentration for a 3 log10 reduction. Peptoids attached via oxazoline or PIII reduced adhesion by > 5 log10 CFU. All covalent methods significantly reduced bacterial adhesion compared to untreated lenses (P < 0.0001). Peptoid-bound lenses were non-toxic to corneal epithelial cells. Sterilization did not affect carbodiimide-treated lenses but reduced the activity of oxazoline and PIII surfaces by 1-2 log10 CFU.

conclusionPeptoids TM5 and TM18 effectively reduced P. aeruginosa adhesion on lenses, with carbodiimide-bound surfaces retaining activity post-sterilization, showing promise for the development of antimicrobial contact lenses.

Indexed as

Bacterial AdhesionContact Lenses, HydrophilicPeptoidsPhotoelectron SpectroscopyPseudomonas aeruginosaEpithelium, CornealEye Infections, BacterialHumansMethacrylatesPseudomonas InfectionsetafilconMethacrylatesPeptoidsAntimicrobial peptoidsContact lensCovalent attachmentMicrobial keratitisP. aeruginosa

Identifiers

PMID39571778
PMCPMC12743605

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Registered trials

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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 OpenQuestion graph.