Evidence map›Paper›PMID 39364796›Full record

ArticlemAbs

A comparative study of the developability of full-length antibodies, fragments, and bispecific formats reveals higher stability risks for engineered constructs.

Itzel Condado-Morales, Fabian Dingfelder, Isabel Waibel, Oliver M Turnbull, Bhargav Patel, Zheng Cao, Jais Rose Bjelke, Susanne Nedergaard Grell, Anja Bennet, Alissa M Hummer and 5 more

Abstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

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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

15 authors.

Itzel Condado-MoralesDepartment of Biophysics and Injectable Formulation, Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
Fabian DingfelderDepartment of Biophysics and Injectable Formulation, Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
Isabel WaibelDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology, Zurich, Switzerland.
Oliver M TurnbullDepartment of Statistics, University of Oxford, Oxford, UK.
Bhargav PatelDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology, Zurich, Switzerland.
Zheng CaoDepartment of Bioanalysis, Beijing Novo Nordisk Pharmaceutical Science & Technology Co. Ltd (Novo Nordisk R&D China), Beijing, China.
Jais Rose BjelkeDepartment of Purification Technologies, Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
Susanne Nedergaard GrellDepartment of Kidney Biology, Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
Anja BennetDepartment of Kidney Biology, Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
Alissa M HummerDepartment of Statistics, University of Oxford, Oxford, UK.
Matthew I J RaybouldDepartment of Statistics, University of Oxford, Oxford, UK.
Charlotte M DeaneDepartment of Statistics, University of Oxford, Oxford, UK.
Thomas EgebjergDepartment of Mammalian Expression, Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
Nikolai LorenzenDepartment of Biophysics and Injectable Formulation, Global Research Technologies, Novo Nordisk A/S, Måløv, Denmark.
Paolo ArosioDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology, Zurich, Switzerland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Engineered antibody formats, such as antibody fragments and bispecifics, have the potential to offer improved therapeutic efficacy compared to traditional full-length monoclonal antibodies (mAbs). However, the translation of these non-natural molecules into successful therapeutics can be hampered by developability challenges. Here, we systematically analyzed 64 different antibody constructs targeting Tumor Necrosis Factor (TNF) which cover 8 distinct molecular format families, encompassing full-length antibodies, various types of single chain variable fragments, and bispecifics. We measured 15 biophysical properties related to activity, manufacturing, and stability, scoring variants with a flag-based risk approach and a recent

Indexed as

Antibodies, BispecificProtein EngineeringProtein StabilitySingle-Chain AntibodiesAntibodies, MonoclonalHumansTumor Necrosis Factor-alphaAntibodies, BispecificAntibodies, MonoclonalSingle-Chain AntibodiesTumor Necrosis Factor-alphaaggregationAntibodyantibody formatsBiophysicsbispecificsColloidal stabilitydevelopabilityFormulationFragmentationfragmentsscFvSelf-associationShelf-life stability

Identifiers

PMID39364796
PMCPMC11457596

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.