Evidence map›Paper›PMID 37916438›Full record

ArticleProtein science : a publication of the Protein Society2023

Lectin-anticancer peptide fusion demonstrates a significant cancer-cell-selective cytotoxic effect and inspires the production of "clickable" anticancer peptide in Escherichia coli.

Rajeev Pasupuleti, Sabrina Riedl, Laia Saltor Núñez, Marianna Karava, Vajinder Kumar, Robert Kourist, W Bruce Turnbull, Dagmar Zweytick, Birgit Wiltschi

Open access · greenAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.4field-weighted citation impact, top 18% of its field
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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
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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

9 authors at 3 institutions in 3 countries.

Rajeev Pasupuletiacib - Austrian Centre of Industrial Biotechnology, Graz, Austria.
Sabrina RiedlInstitute of Molecular Biosciences, Biophysics Division, University of Graz, Graz, Austria.
Laia Saltor NúñezSchool of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.
Marianna KaravaInstitute of Molecular Biotechnology, Graz University of Technology, Graz, Austria.
Vajinder KumarSchool of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.ORCID 0000-0002-8825-3517
Robert KouristInstitute of Molecular Biotechnology, Graz University of Technology, Graz, Austria.
W Bruce TurnbullSchool of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.
Dagmar ZweytickInstitute of Molecular Biosciences, Biophysics Division, University of Graz, Graz, Austria.
Birgit Wiltschiacib - Austrian Centre of Industrial Biotechnology, Graz, Austria.ORCID 0000-0001-5230-0951
Institute of Molecular Biotechnology · ATUniversity of Leeds · GBUniversity of Graz · AT

Funding

Austrian Research Promotion Agency 855671BMK, BMDW, SFG, Standortagentur Tirol, Government of Lower Austria und Vienna Business Agency in the framework of COMET-Competence Centers for Excellent Technologies. The COMET-Funding Program is managed by the Austrian Research Promotion Agency FFG 872161European Union's Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grants 746421European Union's Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grants 814029University of Natural Resources and Life Sciences Vienna (BOKU)
6 · The paper itself

Abstract

Targeted killing of tumor cells while protecting healthy cells is the pressing priority in cancer treatment. Lectins that target a specific glycan marker abundant in cancer cells can be valuable new tools for selective cancer cell killing. The lectin Shiga-like toxin 1 B subunit (Stx1B) is an example that specifically binds globotriaosylceramide (CD77 or Gb3), which is overexpressed in certain cancers. In this study, a human lactoferricin-derived synthetic retro di-peptide R-DIM-P-LF11-215 with antitumor efficacy was fused to the lectin Stx1B to selectively target and kill Gb3+ cancer cells. We produced lectin-peptide fusion proteins in Escherichia coli, isolated them by Gb3-affinity chromatography, and assessed their ability to selectively kill Gb3+ cancer cells in a Calcein AM assay. Furthermore, to expand the applications of R-DIM-P-LF11-215 in developing therapeutic bioconjugates, we labeled R-DIM-P-LF11-215 with the unique reactive non-canonical amino acid N

Indexed as

Antineoplastic AgentsDipeptidesNeoplasmsEscherichia coliHeLa CellsHumansLectinsTrihexosylceramidesAntineoplastic AgentsDipeptidesglobotriaosylceramideLectinsR-DIM-P-LF11Trihexosylceramidesanticancer peptideclick chemistryfusion proteinshuman lactoferricin-derived peptidepeptide purificationrecombinant peptide productiontargeted drug delivery

Identifiers

PMID37916438
PMCPMC10682692
OpenAlexW4388226240

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.