ReviewCancers2026
Biophysical and Structural Characterization of Antibody-Drug Conjugates.
Review in Cancers, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Antibody-drug conjugates (ADCs) comprise a monoclonal antibody covalently bound to a cytotoxic payload by a linker. ADCs minimize off-target effects on healthy tissues, leveraging the specificity of monoclonal antibodies to deliver cytotoxic drugs to the intended tumor site. ADCs can be prone to poor behavior, including aggregation and misfolding, leading to poor efficacy, impaired pharmacokinetics, and immunogenicity. It is advantageous to understand the developability and potential liabilities of a protein candidate prior to costly in vivo studies or clinical trials. This review summarizes biophysical and structural techniques used to characterize ADCs and introduces emerging techniques aimed at accurately assessing the developability of protein candidates. Stability is commonly assayed using techniques like differential scanning calorimetry (DSC), differential scanning fluorimetry (DSF), or spectroscopic probes such as circular dichroism and intrinsic fluorescence. Drug-to-antibody ratio (DAR) is a critical parameter that can be measured using absorbance spectroscopy or chromatographic analysis. Aggregation and self-association can be probed using scattering techniques such as dynamic light scattering (DLS), static light scattering (SLS), and size exclusion chromatography-multi-angle light scattering (SEC-MALS), as well as more specialized approaches such as fluorescence correlation spectroscopy (FCS) and analytical ultracentrifugation (AUC). Mass spectrometry (MS) provides extremely valuable insight into stability, covalent modifications, and, through approaches like hydrogen-deuterium exchange (HDX-MS), structural dynamics of ADCs. Looking forward, the use of biophysical assays in ex vivo matrices and strategic use of artificial intelligence/machine learning (AI/ML) approaches are likely to advance the efficient and rapid development of ADCs and other next-generation protein therapeutics.
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Registered trials
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.