Evidence map›Paper›PMID 40672673›Full record

ArticleACS pharmacology & translational science2025

Comparative Evaluation of Thiol- and Amine-Conjugating Moieties for Endogenous Albumin Binding after Intravenous Administration.

Anja Federa, Hemma Schueffl, Iris K Minichmayr, Alexander Kastner, Julia Kronberger, Thomas L Mindt, Petra Heffeter, Christian R Kowol

Abstract read
In one paragraph

Article in ACS pharmacology & translational science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Exploring the chemical and biological interplay in phenanthroline-containing copper complexes.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  2. Article
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.

Anja FederaInstitute of Inorganic Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Str. 42, A-1090 Vienna, Austria.
Hemma SchuefflCenter for Cancer Research and Comprehensive Cancer Center, Medical University of Vienna, Borschkegasse 8a, A-1090 Vienna, Austria.ORCID https://orcid.org/0000-0002-9959-9716
Iris K MinichmayrDepartment of Clinical Pharmacology, Medical University of Vienna, Waehringer Guertel 18-20, A-1090 Vienna, Austria.
Alexander KastnerInstitute of Inorganic Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Str. 42, A-1090 Vienna, Austria.
Julia KronbergerInstitute of Inorganic Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Str. 42, A-1090 Vienna, Austria.
Thomas L MindtInstitute of Inorganic Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Str. 42, A-1090 Vienna, Austria.ORCID https://orcid.org/0000-0002-2090-1725
Petra HeffeterCenter for Cancer Research and Comprehensive Cancer Center, Medical University of Vienna, Borschkegasse 8a, A-1090 Vienna, Austria.ORCID https://orcid.org/0000-0001-6401-8646
Christian R KowolInstitute of Inorganic Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Str. 42, A-1090 Vienna, Austria.ORCID https://orcid.org/0000-0002-8311-1632

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maleimides are widely used in anticancer drug development for linking small-molecule drugs to macromolecules like antibodies or proteins via thiol-Michael addition reactions. Despite their widespread use, even in clinically approved therapeutics, they present significant drawbacks such as hydrolysis at physiological pH and instability of the formed thiosuccinimide bond. Hence, there is a growing need for more stable yet equally efficient binding units. This is particularly important for drug-delivery systems that bind to endogenous albumin in vivo, exploiting the ability of the protein to accumulate in tumor tissue. This study compares phenyloxadiazolyl methyl sulfone (PODS) and a 2,4-difluorophenyl sulfonamide (DFSA) derivative with maleimide as endogenous albumin binders. Of note, PODS and maleimide bind to Cys34, whereas DFSA targets Lys64 of albumin. The albumin binders were conjugated as axial ligands to oxaliplatin-(IV) complexes (

Indexed as

albuminanticancerdrug deliverymaleimideoxadiazoleplatinum

Identifiers

PMID40672673
PMCPMC12261219

What OpenQuestion holds

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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 OpenQuestion graph.