ArticleBiophysical journal2011
High-throughput analysis of concentration-dependent antibody self-association.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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Who cites it
27 citing papers in PubMed.
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- Protein and Peptide Therapeutics: Stability Challenges, Regulatory Demands, and Innovative Formulation Solutions for Enhanced Clinical Effectiveness.Protein and peptide letters · 2025Review
- DOTAD: A Database of Therapeutic Antibody Developability.Interdisciplinary sciences, computational life sciences · 2024Article
- Profiling the Biophysical Developability Properties of Common IgG1 Fc Effector Silencing Variants.Antibodies (Basel, Switzerland) · 2023Article
- Magnetic field effects on the structure and molecular behavior of pigeon iron-sulfur protein.Protein science : a publication of the Protein Society · 2022Article
- Application of Affinity-Capture Self-Interaction Nanoparticle Spectroscopy in Predicting Protein Stability, Especially for Co-Formulated Antibodies.Pharmaceutical research · 2021Article
- Interaction of clinical-stage antibodies with heme predicts their physiochemical and binding qualities.Communications biology · 2021Article
- SSH: A Tool for Predicting Hydrophobic Interaction of Monoclonal Antibodies Using Sequences.BioMed research international · 2020Article
- Engineering an EGFR-binding Gp2 domain for increased hydrophilicity.Biotechnology and bioengineering · 2019Article
- A Reappraisal of Sedimentation Nonideality Coefficients for the Analysis of Weak Interactions of Therapeutic Proteins.The AAPS journal · 2019Article
- Biophysical properties of the clinical-stage antibody landscape.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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- Article
- Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions.Journal of pharmaceutical sciences · 2014Review
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- Review
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Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies are typically monomeric and nonviscous at low concentrations, yet they display highly variable associative and viscous behavior at elevated concentrations. Although measurements of antibody self-association are critical for understanding this complex behavior, traditional biophysical methods are not capable of characterizing such concentration-dependent self-association in a high-throughput manner. Here we describe a nanoparticle-based method, termed self-interaction nanoparticle spectroscopy, that is capable of rapidly measuring concentration-dependent self-interactions for three human monoclonal antibodies with unique solution behaviors. We demonstrate that gold nanoparticles conjugated with antibodies at low protein concentrations (<40 μg/mL) display self-association behavior (as measured by the interparticle distance-dependent plasmon wavelength) that is well correlated with static light-scattering measurements obtained at three orders of magnitude higher antibody concentrations. Using this methodology, we find that the antibodies display a complex pH-dependent self-association behavior that is strongly influenced by the solution ionic strength. Importantly, we find that a polyclonal human antibody is nonassociative for all solution conditions evaluated in this work, suggesting that antibody self-association is more specific than previously realized. We expect that our findings will guide rational manipulation of antibody phase behavior, and enable studies that elucidate sequence and structural determinants of antibody self-association.
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Registered trials
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