Cited by 9

Nanoplasmonic Avidity‐Based Detection and Quantification of IgG Aggregates

Tran, Thuy, Martinsson, Erik, Vargas, Sergio, Lundström, Ingemar, Mandenius, Carl-Fredrik, Aili, Daniel·2022·Analytical Chemistry

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1021/acs.analchem.2c03446

Cites

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • LSPR biosensors can distinguish aggregates and monomers based on the enhanced apparent affinity of aggregates due to their interactions with multiple ligands.

    “For example, aggregates have enhanced apparent affinity due to their interactions with multiple ligands. Based on this principle, a distinction between aggregates and monomers can be made [97].”

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

No references could be resolved yet.

Research works printed but not linked: 41

  1. Lagassé H. A.; Alexaki A.; Simhadri V. L.; Katagiri N. H.; Jankowski W.; Sauna Z. E.; Kimchi-Sarfaty C. Recent advances in (therapeutic protein) drug development. F1000Res. 2017, 6, 113 10.12688/f1000research.9970.1. 28232867 PMC5302153 · DOI · Paper page
  2. Lu R.-M.; Hwang Y.-C.; Liu I. J.; Lee C.-C.; Tsai H.-Z.; Li H.-J.; Wu H.-C. Development of therapeutic antibodies for the treatment of diseases. J. Biomed. Sci. 2020, 27, 1 10.1186/s12929-019-0592-z. 31894001 PMC6939334 · DOI
  3. Mullard A. 2021 FDA approvals. Nat. Rev. Drug Discov. 2022, 21, 83– 88. 10.1038/d41573-022-00001-9. 34983958 · DOI
  4. Gronemeyer P.; Ditz R.; Strube J. Trends in Upstream and Downstream Process Development for Antibody Manufacturing. Bioengineering 2014, 1, 188– 212. 10.3390/bioengineering1040188. 28955024 · DOI
  5. Gallais Y.; Szely N.; Legrand F. X.; Leroy A.; Pallardy M.; Turbica I. Effect of growth hormone and IgG aggregates on dendritic cells activation and T-cells polarization. Immunol. Cell Biol. 2017, 95, 306– 315. 10.1038/icb.2016.100. 27713394 · DOI
  6. Lundahl M. L. E.; Fogli S.; Colavita P. E.; Scanlan E. M. Aggregation of protein therapeutics enhances their immunogenicity: causes and mitigation strategies. RSC Chem. Biol. 2021, 2, 1004– 1020. 10.1039/D1CB00067E. 34458822 PMC8341748 · DOI · Paper page
  7. Moussa E. M.; Panchal J. P.; Moorthy B. S.; Blum J. S.; Joubert M. K.; Narhi L. O.; Topp E. M. Immunogenicity of Therapeutic Protein Aggregates. J. Pharm. Sci. 2016, 105, 417– 430. 10.1016/j.xphs.2015.11.002. 26869409 · DOI
  8. Tada M.; Aoyama M.; Ishii-Watabe A. Fcγ Receptor Activation by Human Monoclonal Antibody Aggregates. J. Pharm. Sci. 2020, 109, 576– 583. 10.1016/j.xphs.2019.10.046. 31676270 · DOI
  9. Vázquez-Rey M.; Lang D. A. Aggregates in monoclonal antibody manufacturing processes. Biotechnol. Bioeng. 2011, 108, 1494– 1508. 10.1002/bit.23155. 21480193 · DOI
  10. Capito F.; Skudas R.; Kolmar H.; Hunzinger C. Mid-infrared spectroscopy-based antibody aggregate quantification in cell culture fluids. Biotechnol. J. 2013, 8, 912– 917. 10.1002/biot.201300164. 23712876 · DOI
  11. Wang W.; Singh S.; Zeng D. L.; King K.; Nema S. Antibody structure, instability, and formulation. J. Pharm. Sci. 2007, 96, 1– 26. 10.1002/jps.20727. 16998873 · DOI
  12. Goyon A.; D’Atri V.; Colas O.; Fekete S.; Beck A.; Guillarme D. Characterization of 30 therapeutic antibodies and related products by size exclusion chromatography: Feasibility assessment for future mass spectrometry hyphenation. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2017, 1065-1066, 35– 43. 10.1016/j.jchromb.2017.09.027. 28946123 · DOI
  13. Mahler H.-C.; Friess W.; Grauschopf U.; Kiese S. Protein aggregation: Pathways, induction factors and analysis. J. Pharm. Sci. 2009, 98, 2909– 2934. 10.1002/jps.21566. 18823031 · DOI
  14. Bansal R.; Gupta S.; Rathore A. S. Analytical Platform for Monitoring Aggregation of Monoclonal Antibody Therapeutics. Pharm. Res. 2019, 36, 152 10.1007/s11095-019-2690-8. 31463609 · DOI
  15. Fekete S.; Beck A.; Veuthey J.-L.; Guillarme D. Theory and practice of size exclusion chromatography for the analysis of protein aggregates. J. Pharm. Biomed. Anal. 2014, 101, 161– 173. 10.1016/j.jpba.2014.04.011. 24816223 · DOI
  16. Sahin E.; Roberts C. J. Size-exclusion chromatography with multi-angle light scattering for elucidating protein aggregation mechanisms. Methods Mol. Biol. 2012, 899, 403– 423. 10.1007/978-1-61779-921-1_25. 22735967 · DOI
  17. Bou-Assaf G. M.; Budyak I. L.; Brenowitz M.; Day E. S.; Hayes D.; Hill J.; Majumdar R.; Ringhieri P.; Schuck P.; Lin J. C. Best Practices for Aggregate Quantitation of Antibody Therapeutics by Sedimentation Velocity Analytical Ultracentrifugation. J. Pharm. Sci. 2022, 111, 2121– 2133. 10.1016/j.xphs.2021.12.023. 34986360 PMC9232890 · DOI
  18. Gabrielson J. P.; Brader M. L.; Pekar A. H.; Mathis K. B.; Winter G.; Carpenter J. F.; Randolph T. W. Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity. J. Pharm. Sci. 2007, 96, 268– 279. 10.1002/jps.20760. 17080424 · DOI
  19. Rathore A. S.; Bhambure R.; Ghare V. Process analytical technology (PAT) for biopharmaceutical products. Anal. Bioanal. Chem. 2010, 398, 137– 154. 10.1007/s00216-010-3781-x. 20480150 · DOI
  20. McAvan B. S.; Bowsher L. A.; Powell T.; O’Hara J. F.; Spitali M.; Goodacre R.; Doig A. J. Raman Spectroscopy to Monitor Post-Translational Modifications and Degradation in Monoclonal Antibody Therapeutics. Anal. Chem. 2020, 92, 10381– 10389. 10.1021/acs.analchem.0c00627. 32614170 PMC7467412 · DOI · Paper page
  21. Zhang C.; Springall J. S.; Wang X.; Barman I. Rapid, quantitative determination of aggregation and particle formation for antibody drug conjugate therapeutics with label-free Raman spectroscopy. Anal. Chim. Acta 2019, 1081, 138– 145. 10.1016/j.aca.2019.07.007. 31446951 PMC6750807 · DOI
  22. Tran T.; Eskilson O.; Mayer F.; Gustavsson R.; Selegård R.; Lundström I.; Mandenius C.-F.; Martinsson E.; Aili D. Real-Time Nanoplasmonic Sensor for IgG Monitoring in Bioproduction. Processes 2020, 8, 1302 10.3390/pr8101302. · DOI · Paper page
  23. Lee S.; Song H.; Ahn H.; Kim S.; Choi J.-R.; Kim K. Fiber-Optic Localized Surface Plasmon Resonance Sensors Based on Nanomaterials. Sensors (Basel) 2021, 21, 819 10.3390/s21030819. 33530416 PMC7865415 · DOI
  24. Svedendahl M.; Chen S.; Dmitriev A.; Käll M. Refractometric Sensing Using Propagating versus Localized Surface Plasmons: A Direct Comparison. Nano Lett. 2009, 9, 4428– 4433. 10.1021/nl902721z. 19842703 · DOI
  25. Unser S.; Bruzas I.; He J.; Sagle L. Localized Surface Plasmon Resonance Biosensing: Current Challenges and Approaches. Sensors 2015, 15, 15684 10.3390/s150715684. 26147727 PMC4541850 · DOI
  26. Jain K.; Salamat-Miller N.; Taylor K. Freeze-thaw characterization process to minimize aggregation and enable drug product manufacturing of protein based therapeutics. Sci. Rep. 2021, 11, 11332 10.1038/s41598-021-90772-9. 34059716 PMC8166975 · DOI
  27. Liu J.; Nguyen M. D. H.; Andya J. D.; Shire S. J. Reversible Self-Association Increases the Viscosity of a Concentrated Monoclonal Antibody in Aqueous Solution. J. Pharm. Sci. 2005, 94, 1928– 1940. 10.1002/jps.20347. 16052543 · DOI
  28. Choe W.; Durgannavar T. A.; Chung S. J. Fc-Binding Ligands of Immunoglobulin G: An Overview of High Affinity Proteins and Peptides. Materials 2016, 9, 994 10.3390/ma9120994. PMC5456964 28774114 · DOI
  29. Mazzer A. R.; Perraud X.; Halley J.; O’Hara J.; Bracewell D. G. Protein A chromatography increases monoclonal antibody aggregation rate during subsequent low pH virus inactivation hold. J. Chromatogr. A 2015, 1415, 83– 90. 10.1016/j.chroma.2015.08.068. 26346187 PMC4582070 · DOI
  30. Page M.; Thorpe R. Purification of IgG Using Protein A or Protein G. In The Protein Protocols Handbook, Walker J. M. Ed.; Humana Press: Totowa, NJ, 2002; 993– 994.
  31. Moks T.; Abrahmsén L.; Nilsson B.; Hellman U.; Sjöquist J.; Uhlén M. Staphylococcal protein A consists of five IgG-binding domains. Eur. J. Biochem. 1986, 156, 637– 643. 10.1111/j.1432-1033.1986.tb09625.x. 2938951 · DOI
  32. Inganäs M.; Johansson S. G.; Bennich H. H. Interaction of human polyclonal IgE and IgG from different species with protein A from Staphylococcus aureus: demonstration of protein-A-reactive sites located in the Fab’2 fragment of human IgG. Scand. J. Immunol. 1980, 12, 23– 31. 10.1111/j.1365-3083.1980.tb00037.x. 6158089 · DOI
  33. Jansson B.; Uhlén M.; Nygren P.-Å. All individual domains of staphylococcal protein A show Fab binding. FEMS Immunol. Med. Microbiol. 1998, 20, 69– 78. 10.1016/S0928-8244(97)00108-9. 9514577 · DOI
  34. Mo J.; Yan Q.; So C. K.; Soden T.; Lewis M. J.; Hu P. Understanding the Impact of Methionine Oxidation on the Biological Functions of IgG1 Antibodies Using Hydrogen/Deuterium Exchange Mass Spectrometry. Anal. Chem. 2016, 88, 9495– 9502. 10.1021/acs.analchem.6b01958. 27575380 · DOI
  35. Karlsson R.; Fält A. Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 1997, 200, 121– 133. 10.1016/S0022-1759(96)00195-0. 9005951 · DOI
  36. Saha K.; Bender F.; Gizeli E. Comparative Study of IgG Binding to Proteins G and A: Nonequilibrium Kinetic and Binding Constant Determination with the Acoustic Waveguide Device. Anal. Chem. 2003, 75, 835– 842. 10.1021/ac0204911. 12622374 · DOI
  37. Bronner V.; Tabul M.; Bravman T. Rapid Screening and Selection of Optimal Antibody Capturing Agents Using the ProteOn XPR36 Protein Interaction Array System; BioRad Laboratories. Inc. Bulletin 2009, 5820.
  38. Farooq S.; Wali F.; Zezell D. M.; de Araujo R. E.; Rativa D. Optimizing and Quantifying Gold Nanospheres Based on LSPR Label-Free Biosensor for Dengue Diagnosis. Polymer 2022, 14, 1592 10.3390/polym14081592. PMC9031946 35458342 · DOI
  39. Martinsson E.; Shahjamali M. M.; Enander K.; Boey F.; Xue C.; Aili D.; Liedberg B. Local Refractive Index Sensing Based on Edge Gold-Coated Silver Nanoprisms. J. Phys. Chem. C 2013, 117, 23148– 23154. 10.1021/jp408187e. · DOI
  40. Luo Y.; Lu Z.; Raso S. W.; Entrican C.; Tangarone B. Dimers and multimers of monoclonal IgG1 exhibit higher in vitro binding affinities to Fcgamma receptors. mAbs 2009, 1, 491– 504. 10.4161/mabs.1.5.9631. 20065648 PMC2759499 · DOI
  41. Segal D. M.; Hurwitz E. Binding of Affinity Cross-Linked Oligomers of IgG to Cells Bearing Fc Receptors. J. Immunol. 1977, 118, 1338. 66289

Cited by

Sorted by citations

Authors
Tran, T., Martinsson, E., Vargas, S., Lundström, I., Mandenius, C.-F., & Aili, D.
Affiliations
  • Laboratory of Molecular Materials, Division of Biophysics and Bioengineering, Department of Physics, Chemistry and Biology, Linköping University, Linköping 581 83, Sweden
  • ArgusEye AB, Spannmålsgatan 55, Linköping 583 36, Sweden
  • Wolfram MathCore AB, Teknikringen 1E, Linköping 583 30, Sweden
  • Sensor and Actuator Systems, Department of Physics, Chemistry and Biology, Linköping University, Linköping 581 83, Sweden
  • Biotechnology, Division of Biophysics and Bioengineering, Department of Physics, Chemistry and Biology, Linköping University, Linköping 581 83, Sweden
Venue
Analytical Chemistry
Published
2022-11-01
Volume
94
Issue
45
Pages
15754-15762
ISSN
  • 0003-2700
  • 1520-6882
Cited by
9
References
0
Language
en
Funders
  • Vetenskapsr?det (2016-04120, 2019-00130)
  • VINNOVA
  • H2020 Marie Sklodowska-Curie Actions (841373)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review