ArticleEuropean journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V2015
The second virial coefficient as a predictor of protein aggregation propensity: A self-interaction chromatography study.
Article in European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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.
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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.
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Who cites it
29 citing papers in PubMed, 84 citations in OpenAlex.
- Monomeric Insulin Analog and Stabilizing Excipient Enabled Ultrafast Insulin Formulation.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Emerging Technologies and Integrated Interdisciplinary Strategies for Mitigating Protein Aggregation in Therapeutic Formulations.Pharmaceutical research · 2026Review
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- Preserved bevacizumab (Avastin®) eye drops for application in multidose containers - an in-vitro characterisation.BMC veterinary research · 2025Article
- Polymethylenetetrazole: Synthesis, Characterization, and Energetic Properties.Molecules (Basel, Switzerland) · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain.The European physical journal. E, Soft matter · 2024Article
- Article
- Combined Effects of Pressure and Ionic Strength on Protein-Protein Interactions: An Empirical Approach.Biomacromolecules · 2024Article
- Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.RSC advances · 2023Review
- The origins of nonideality exhibited by monoclonal antibodies and Fab fragments in human serum.Protein science : a publication of the Protein Society · 2023Article
- The ins and outs of membrane bending by intrinsically disordered proteins.Science advances · 2023Article
- Electrostatics Drive Oligomerization and Aggregation of Human Interferon Alpha-2a.The journal of physical chemistry. B · 2021Article
- Probing interactions of therapeutic antibodies with serum via second virial coefficient measurements.Biophysical journal · 2021Article
- Effect of Buffer on Protein Stability in Aqueous Solutions: A Simple Protein Aggregation Model.The journal of physical chemistry. B · 2021Article
- Protein aggregation and immunogenicity of biotherapeutics.International journal of pharmaceutics · 2020Review
- Calculation of Second Virial Coefficients of Atomistic Proteins Using Fast Fourier Transform.The journal of physical chemistry. B · 2019Article
- A Reappraisal of Sedimentation Nonideality Coefficients for the Analysis of Weak Interactions of Therapeutic Proteins.The AAPS journal · 2019Article
- Improved adsorption reactions, kinetics and stability for model and therapeutic proteins immobilised on affinity resins.Adsorption : journal of the International Adsorption Society · 2019Article
- On the Colloidal Stability of Spherical Copolymeric Micelles.ACS omega · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The second osmotic virial coefficients (b2) of four proteins - lysozyme, recombinant human lactoferrin, concanavalin A and catalase were measured by self-interaction chromatography (SIC) in solutions of varying salt type, concentration and pH. Protein aggregate sizes based on the initial hydrodynamic radius of the protein solution species present were measured using dynamic light scattering, and the relationship between b2 and protein aggregate size was studied. A linear correlation was established between b2 values and protein aggregate hydrodynamic size for all proteins, and for almost all solution conditions. Aggregate sizes of <∼10nm, indicative of non-aggregated protein systems, were consistently observed to have b2 values >0. The observed b2 trends as a function of solution conditions were very much protein dependent, with notable trends including the existence of attractive interactions (negative b2 values) at low ionic strengths for catalase and concanavalin A, and the highly positive b2 values observed for lactoferrin over a wide range of solution conditions, reflecting lactoferrin's innately high stability. It is concluded that the quantification of protein-protein interactions using SIC based b2 data is a potentially valuable screening tool for predicting protein aggregation propensity.
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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 OpenQuestion graph.