Evidence map›Paper›PMID 42736492›Full record

ArticleThe AAPS journal2026

Real-Time Single-Aggregate Analysis of Vaccine Antigen Stability via Stochastic Electrochemical Blocking.

Kathryn G Shields, Azaria A Wagner, Morgan F Rudesill, Weiyue Xin, Emory M Payne, Jeffrey E Dick

Abstract read
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In one paragraph

Article in The AAPS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

6 authors.

Kathryn G Shields *Department of Chemistry, James Tarpo Jr. and Margaret Tarpo, Purdue University, West Lafayette, Indiana, 47907, USA.
Azaria A Wagner *Department of Chemistry, James Tarpo Jr. and Margaret Tarpo, Purdue University, West Lafayette, Indiana, 47907, USA.
Morgan F RudesillDepartment of Chemistry, James Tarpo Jr. and Margaret Tarpo, Purdue University, West Lafayette, Indiana, 47907, USA.
Weiyue XinAnalytical Research and Development, Merck & Co., Inc., 126 E. Lincoln Ave., Rahway, New Jersey, 07065, USA.
Emory M PayneAnalytical Research and Development, Merck & Co., Inc., 126 E. Lincoln Ave., Rahway, New Jersey, 07065, USA. emory.payne@merck.com.ORCID http://orcid.org/0000-0002-5956-8392
Jeffrey E DickDepartment of Chemistry, James Tarpo Jr. and Margaret Tarpo, Purdue University, West Lafayette, Indiana, 47907, USA. jdick@purdue.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregation remains a major challenge in vaccine stability, particularly for protein antigens that undergo structural perturbation during storage, reconstitution, and transport. Here, we apply stochastic electrochemical blocking to observe aggregation of the glycoprotein E (gE) antigen from the SHINGRIX™ vaccine under different formulation and temperature conditions. This orthogonal technique to more traditional light-based methods enables rapid, single-particle, qualitative measurements in solution without introducing shear forces or nonnative interfaces. We examined gE aggregates after reconstitution over a two-week period via additions of MilliQ water, the buffer matrix of the liposome-based adjuvant AS01

Indexed as

AntigensElectrochemical TechniquesProtein AggregatesVaccinesDrug StabilityLiposomesStochastic ProcessesTemperatureAntigensLiposomesProtein AggregatesVaccinesadjuvant–antigen interactionsAS01B adjuvantelectrochemical blockingformulation scienceglycoprotein E (gE) antigenprotein aggregationSHINGRIX™stochastic electrochemistrytemperature stabilityvaccine stability

Identifiers

PMID42736492

What OpenQuestion holds

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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.