Evidence map›Paper›PMID 27362833›Full record

ArticlemAbs2016

Comparison of originator and biosimilar therapeutic monoclonal antibodies using comprehensive two-dimensional liquid chromatography coupled with time-of-flight mass spectrometry.

Matthew Sorensen, David C Harmes, Dwight R Stoll, Gregory O Staples, Szabolcs Fekete, Davy Guillarme, Alain Beck

Open access · goldAbstract readComparative Study
In one paragraph

Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

16 citing papers in PubMed, 87 citations in OpenAlex.

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  8. Recombinant Proteins and Monoclonal Antibodies.Advances in biochemical engineering/biotechnology · 2021
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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

7 authors at 4 institutions in 3 countries.

Matthew Sorensena Gustavus Adolphus College , Department of Chemistry , St. Peter , MN , USA.
David C Harmesa Gustavus Adolphus College , Department of Chemistry , St. Peter , MN , USA.
Dwight R Stolla Gustavus Adolphus College , Department of Chemistry , St. Peter , MN , USA.
Gregory O Staplesb Agilent Technologies , Santa Clara , CA , USA.
Szabolcs Feketec School of Pharmaceutical Sciences, University of Geneva, University of Lausanne, Boulevard d'Yvoy , Geneva , Switzerland.
Davy Guillarmec School of Pharmaceutical Sciences, University of Geneva, University of Lausanne, Boulevard d'Yvoy , Geneva , Switzerland.
Alain Beckd Center of Immunology Pierre Fabre , Saint-Julien-en-Genevois , France.
Gustavus Adolphus College · USUniversity of Geneva · CHAgilent Technologies (United States) · USCenter of Immunology Pierre Fabre · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As research, development, and manufacturing of biosimilar protein therapeutics proliferates, there is great interest in the continued development of a portfolio of complementary analytical methods that can be used to efficiently and effectively characterize biosimilar candidate materials relative to the respective reference (i.e., originator) molecule. Liquid phase separation techniques such as liquid chromatography and capillary electrophoresis are powerful tools that can provide both qualitative and quantitative information about similarities and differences between reference and biosimilar materials, especially when coupled with mass spectrometry. However, the inherent complexity of these protein materials challenges even the most modern one-dimensional (1D) separation methods. Two-dimensional (2D) separations present a number of potential advantages over 1D methods, including increased peak capacity, 2D peak patterns that can facilitate unknown identification, and improvement in the compatibility of some separation methods with mass spectrometry. In this study, we demonstrate the use of comprehensive 2D-LC separations involving cation-exchange (CEX) and reversed-phase (RP) separations in the first and second dimensions to compare 3 reference/biosimilar pairs of monoclonal antibodies (cetuximab, trastuzumab and infliximab) that cover a range of similarity/disimilarity in a middle-up approach. The second dimension RP separations are coupled to time-of-flight mass spectrometry, which enables direct identification of features in the chromatograms obtained from mAbs digested with the IdeS enzyme, or digestion with IdeS followed by reduction with dithiothreitol. As many as 23 chemically unique mAb fragments were detected in a single sample. Our results demonstrate that these rich datasets enable facile assesment of the degree of similarity between reference and biosimilar materials.

Indexed as

Antibodies, MonoclonalBiosimilar PharmaceuticalsChromatography, LiquidMass SpectrometryAntibodies, MonoclonalBiosimilar PharmaceuticalsBiosimilarscation-exchangemass spectrometrymiddle-up analysismonoclonal antibodiesreversed-phasetwo-dimensional liquid chromatography

Identifiers

PMID27362833
PMCPMC5058618
OpenAlexW2466024678

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.