Evidence map›Paper›PMID 31446951›Full record

ArticleAnalytica chimica acta2019

Rapid, quantitative determination of aggregation and particle formation for antibody drug conjugate therapeutics with label-free Raman spectroscopy.

Chi Zhang, Jeremy S Springall, Xiangyang Wang, Ishan Barman

Abstract read
In one paragraph

Article in Analytica chimica acta, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Multiplexed SERS Detection of Serum Cardiac Markers Using Plasmonic Metasurfaces.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
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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

4 authors.

Chi ZhangDepartment of Mechanical Engineering, Johns Hopkins University, Baltimore, MD, USA.
Jeremy S SpringallAstraZeneca, R&D Biopharmaceuticals, Biopharmaceutical Product Development, Analytical Sciences, Gaithersburg, MD, USA. Electronic address: springallj@MedImmune.com.
Xiangyang WangAstraZeneca, R&D Biopharmaceuticals, Biopharmaceutical Product Development, Analytical Sciences, Gaithersburg, MD, USA.
Ishan BarmanDepartment of Mechanical Engineering, Johns Hopkins University, Baltimore, MD, USA; Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, MD, USA; Department of Radiology & Radiological Science, Johns Hopkins University School of Medicine, Baltimore, MD, USA. Electronic address: ibarman@jhu.edu.

Funding

Wide-Field Short-Wave Infrared (SWIR) multiphoton (MP) tissue imagingP41EB015871 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SO, PETER T. · 2012 to 2021
$11.3M
Spectroscopy assisted mechano-chemical phenotype recognition nanoscopeDP2GM128198 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARMAN, ISHAN · 2017 to 2017
$2.5M
NIBIB NIH HHS P41 EB015871NIGMS NIH HHS DP2 GM128198
6 · The paper itself

Abstract

Lot release and stability testing of biologics are essential parts of the quality control strategy for ensuring therapeutic material dosed to patients is safe and efficacious, and consistent with previous clinical and toxicological experience. Characterization of protein aggregation is of particular significance, as aggregates may lose the intrinsic pharmaceutical properties as well as engage with the immune system instigating undesirable downstream immunogenicity. While important, real-time identification and quantification of subvisible particles in the monoclonal antibody (mAb) drug products remains inaccessible with existing techniques due to limitations in measurement time, sensitivity or experimental conditions. Here, owing to its exquisite molecular specificity, non-perturbative nature and lack of sample preparation requirements, we propose label-free Raman spectroscopy in conjunction with multivariate analysis as a solution to this unmet need. By leveraging subtle, but consistent, differences in vibrational modes of the biologics, we have developed a support vector machine-based regression model that provides fast, accurate prediction for a wide range of protein aggregations. Moreover, in blinded experiments, the model shows the ability to precisely differentiate between aggregation levels in mAb like product samples pre- and post-isothermal incubation, where an increase in aggregate levels was experimentally determined. In addition to offering fresh insights into mAb like product-specific aggregation mechanisms that can improve engineering of new protein therapeutics, our results highlight the potential of Raman spectroscopy as an in-line analytical tool for monitoring protein particle formation.

Indexed as

Protein AggregatesAlgorithmsAntibodies, MonoclonalImmunoconjugatesMultivariate AnalysisPrincipal Component AnalysisProtein MultimerizationRegression AnalysisSpectrum Analysis, RamanSupport Vector MachineAntibodies, MonoclonalImmunoconjugatesProtein AggregatesProtein aggregationRaman spectroscopySupport vector machine

Identifiers

PMID31446951
PMCPMC6750807

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Registered trials

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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.