Research &
publications.

Research & publications

Novartis case study2026Protein formulation developmentInternational Journal of PharmaceuticsView at publisher ↗

Novartis case study

Biopharmaceutical development

Advancing biophysics: semi-automated monitoring of protein aggregation kinetics to complement development of biopharmaceutics

Thorben Höltkemeier, Cédric Thauvin, Jason Allison, Dario Spigolon, Sorina Morar-Mitrica, Niklas Meier, Ingo Fischer, Karoline Bechtold-Peters & Wolfgang Friess

International Journal of Pharmaceutics · 2026 · 127621 · Online 31 October

Study finding
Automated analysis reduced operator-related variation. Three case studies examined buffer, pH and excipient choices under thermal and stirring stress.

Relevance to ARGEN
Evaluates SMSLS, the measurement approach underlying ARGEN, for protein formulation decisions. Findings apply to the studied samples and conditions.

Publisher ↗PubMed ↗

DOI: 10.1016/j.ijpharm.2026.127621

Full text available through the publisher. Access terms may apply.

Research reference2013Monitoring aggregation kineticsAnalytical BiochemistryView at publisher ↗

SMSLS foundation

Protein aggregation

Monitoring protein aggregation kinetics with simultaneous multiple sample light scattering

Michael F. Drenski, Mark L. Brader, Roy W. Alston & Wayne F. Reed

Analytical Biochemistry · 2013 · 437: 185–197

Study finding
A multi-sample prototype tracked early aggregation of two monoclonal antibodies across temperature and concentration conditions, revealing distinct kinetic regimes.

Relevance to ARGEN
Foundational work on the SMSLS method underlying ARGEN; the paper describes a research prototype.

Publisher ↗

DOI: 10.1016/j.ab.2013.02.014

Full text available through the publisher. Access terms may apply.

Research reference2015Continuous monitoring methodsACS Symposium SeriesView at publisher ↗

SMSLS foundation

Methods & stress testing

Simultaneous Multiple Sample Light Scattering (SMSLS) for Continuous Monitoring of Protein Aggregation

Michael F. Drenski, Mark L. Brader & Wayne F. Reed

ACS Symposium Series · 2015 · 1202, Chapter 6: 159–188

Study finding
This book chapter describes continuous monitoring of NISTmAb and industrial antibodies under thermal and stirring stress, including air–liquid interface effects.

Relevance to ARGEN
Explains the method and experimental approach. Its 16-cell prototype is not a specification for the current ARGEN configuration.

Publisher ↗

DOI: 10.1021/bk-2015-1202.ch006

Full text available through the publisher. Access terms may apply.

ARGEN study

mRNA stability

Consequences of mRNA Secondary Structure on Stability against both Hydrolysis and Aggregation: The Role of Electrostatic, π–π Stacking, and Thermal Effects

Curtis W. Jarand, Zhiyou Deng, Mark L. Brader & Wayne F. Reed

ACS Omega · 2026 · 11(3): 4440–4456

Study finding
Studies of free mRNA linked secondary structure to resistance against hydrolysis and aggregation, with responses varying by RNA and solution conditions.

Relevance to ARGEN
Methods explicitly use ARGEN for static light scattering alongside DLS and a custom dialysis device. This is free-mRNA research, not LNP formulation validation.

Read PDF ↗Publisher ↗

DOI: 10.1021/acsomega.5c10266

© 2026 The Authors. Published by American Chemical Society.
Licensed under CC BY 4.0.
Thumbnail: reduced-size article opening page. PDF unchanged.

Research reference2018Understanding reproducibilityThe Journal of Physical Chemistry BView at publisher ↗

ARGEN study

Aggregation reproducibility

On the Reproducibility of Early-Stage Thermally Induced and Contact-Stir-Induced Protein Aggregation

Curtis W. Jarand & Wayne F. Reed

The Journal of Physical Chemistry B · 2018 · 122(40): 9361–9372

Study finding
For BSA and one monoclonal antibody, thermal aggregation was reproducible within instrumental error, while contact-stir aggregation showed greater variability.

Relevance to ARGEN
Uses ARGEN to distinguish measurement uncertainty from variability in the aggregation process under the tested conditions.

Publisher ↗

DOI: 10.1021/acs.jpcb.8b07820

Full text available through the publisher. Access terms may apply.

ARGEN + custom method

Equilibrium characterization

Automatic, single-sweep, cuvette-based determination of A₂ (B₂₂), Kᴅ, and other equilibrium properties for macromolecules

Curtis W. Jarand & Wayne F. Reed

Measurement Science and Technology · 2026 · 37: 305701

Study finding
An automatic continuous-dilution method measured concentration-dependent properties of proteins and polysaccharides in a single cuvette.

Relevance to ARGEN
ARGEN supplied static-scattering measurements of molar mass and A₂. Kᴅ came from a separate DLS instrument; the study used custom dilution hardware.

Read PDF ↗Publisher ↗

DOI: 10.1088/1361-6501/ae8923

© 2026 The Authors. Published by IOP Publishing Ltd.
Licensed under CC BY 4.0.
Thumbnail: reduced-size article opening page. PDF unchanged.

ARGEN study

Peptide stability

Anisotropic Electrostatics in the Instability of GLP-1 Analog Micelles: Effects of Electrolytes, Denaturants, pH, and Temperature

Curtis W. Jarand, Ivan Zemskov, David Müller, Andreas Stadelmaier, Laurin Melzig, Ralph Schönleber & Wayne F. Reed

ACS Omega · 2026 · 11: 49381–49401

Study finding
Liraglutide and semaglutide experiments linked aggregation to electrolyte-dependent electrostatic interactions and mapped responses to denaturant and pH.

Relevance to ARGEN
Uses ARGEN static light scattering alongside DLS and custom dialysis to investigate GLP-1 analog solution stability.

Read PDF ↗Publisher ↗

DOI: 10.1021/acsomega.6c02639

© 2026 The Authors. Published by American Chemical Society.
Licensed under CC BY 4.0.
Thumbnail: reduced-size article opening page. PDF unchanged.

Findings apply to each study’s samples, methods and conditions. Research instruments and custom accessories may differ from the current commercial configuration. Open-access PDFs and previews are credited under CC BY 4.0. Other publications link to their publisher records. Inclusion does not imply endorsement by the authors or publishers.