Salt-dependent passive adsorption of IgG1κ-type monoclonal antibodies on hydrophobic microparticles

Džupponová, Veronika

doi:10.1016/j.bpc.2021.106609

Cited by 5 publications

(3 citation statements)

References 42 publications

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“…In our study, the examination of the IgG antibody adsorption process, revealed by experimental and computational outcomes, indicated a consistent observation of antibody adsorption occurring preferentially in an extended configuration over the mica substrate. This orientation is suggested to be influenced by surface chemistry, the presence of other proteins, salinity, and pH conditions [ 23 , 37 , 38 , 39 ]. The relationship between IgG orientation on solid surfaces and antigen binding capacity is of interest [ 23 , 40 , 41 ]; for example, Xu H et al (2006) [ 23 ] revealed an increased steric hindrance with a higher antibody packing density, affecting hCG binding.…”

Section: Discussionmentioning

confidence: 99%

The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation

Santander,

Bravo,

Chang-Halabi

et al. 2023

IJMS

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The adsorption of proteins onto surfaces significantly impacts biomaterials, medical devices, and biological processes. This study aims to provide insights into the irreversible adsorption process of multiprotein complexes, particularly focusing on the interaction between anti-His6 IgG antibodies and the His6-tagged P2X2 receptor. Traditional approaches to understanding protein adsorption have centered around kinetic and thermodynamic models, often examining individual proteins and surface coverage, typically through Molecular Dynamics (MD) simulations. In this research, we introduce a computational approach employing Autodesk Maya 3D software for the investigation of multiprotein complexes’ adsorption behavior. Utilizing Atomic Force Microscopy (AFM) imaging and Maya 3D-based mechanical simulations, our study yields real-time structural and kinetic observations. Our combined experimental and computational findings reveal that the P2X2 receptor–IgG antibody complex likely undergoes absorption in an ‘extended’ configuration. Whereas the P2X2 receptor is less adsorbed once is complexed to the IgG antibody compared to its individual state, the opposite is observed for the antibody. This insight enhances our understanding of the role of protein–protein interactions in the process of protein adsorption.

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Section: Discussionmentioning

confidence: 99%

The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation

Santander,

Bravo,

Chang-Halabi

et al. 2023

IJMS

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“…Therefore, the hydrophobic interface is more conducive to direct physical adsorption of antibodies. This is important for the construction of biosensors, because the additional complexity involved in chemical treatment can be avoided ( Dzupponova and Zoldak, 2021 ).…”

Section: Biosensors Based On Non-covalent Interactions On the Surface...mentioning

confidence: 99%

A Review of Transition Metal Dichalcogenides-Based Biosensors

Sun

Yue

et al. 2022

Front. Bioeng. Biotechnol.

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Transition metal dichalcogenides (TMDCs) are widely used in biosensing applications due to their excellent physical and chemical properties. Due to the properties of biomaterial targets, the biggest challenge that biosensors face now is how to improve the sensitivity and stability. A lot of materials had been used to enhance the target signal. Among them, TMDCs show excellent performance in enhancing biosensing signals because of their metallic and semi-conducting electrical capabilities, tunable band gap, large specific surface area and so on. Here, we review different functionalization methods and research progress of TMDCs-based biosensors. The modification methods of TMDCs for biosensor fabrication mainly include two strategies: non-covalent and covalent interaction. The article summarizes the advantages and disadvantages of different modification strategies and their effects on biosensing performance. The authors present the challenges and issues that TMDCs need to be addressed in biosensor applications. Finally, the review expresses the positive application prospects of TMDCs-based biosensors in the future.

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“…Despite the vast potential and numerous benefits to pharmaceutical research, protein microcrystals demonstrate challenges for structural characterization at high resolution in native formulation due to relatively small particle size, aqueous environment, and multicomponent nature. Similar to small-molecule crystals, solid-state characterization techniques to characterize protein microcrystals include dynamic light scattering, differential scanning calorimetry (DSC), infrared spectroscopy, scanning and transmission electron microscopy, , powder X-ray diffraction (PXRD), atomic force microscopy (AFM), Fourier transform infrared (FTIR) spectroscopy, solid-state NMR spectroscopy (ssNMR), − and many others. ,− For example, AFM enables investigation of particle surfaces and characterization of the crystallization process . Particle size distribution can also be analyzed by laser diffraction techniques .…”

Section: Introductionmentioning

confidence: 99%

Investigating Crystalline Protein Suspension Formulations of Pembrolizumab from MAS NMR Spectroscopy

Reichert

Narasimhan

et al. 2022

Mol. Pharmaceutics

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Developing biological formulations to maintain the chemical and structural integrity of therapeutic antibodies remains a significant challenge. Monoclonal antibody (mAb) crystalline suspension formulation is a promising alternative for high concentration subcutaneous drug delivery. It demonstrates many merits compared to the solution formulation to reach a high concentration at the reduced viscosity and enhanced stability. One main challenge in drug development is the lack of high-resolution characterization of the crystallinity and stability of mAb microcrystals in the native formulations. Conventional analytical techniques often cannot evaluate structural details of mAb microcrystals in the native suspension due to the presence of visible particles, relatively small crystal size, high protein concentration, and multicomponent nature of a liquid formulation. This study demonstrates the first high-resolution characterization of mAb microcrystalline suspension using magic angle spinning (MAS) NMR spectroscopy. Crystalline suspension formulation of pembrolizumab (Keytruda, Merck & Co., Inc., Kenilworth, NJ 07033, U.S.) is utilized as a model system. Remarkably narrow 13 C spectral linewidth of approximately 29 Hz suggests a high order of crystallinity and conformational homogeneity of pembrolizumab crystals. The impact of thermal stress and dehydration on the structure, dynamics, and stability of these mAb crystals in the formulation environment is evaluated. Moreover, isotopic labeling and heteronuclear 13 C and 15 N spectroscopies have been utilized to identify the binding of caffeine in the pembrolizumab crystal lattice, providing molecular insights into the cocrystallization of the protein and ligand. Our study provides valuable structural details for facilitating the design of crystalline suspension formulation of Keytruda and demonstrates the high potential of MAS NMR as an advanced tool for biophysical characterization of biological therapeutics.

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Salt-dependent passive adsorption of IgG1κ-type monoclonal antibodies on hydrophobic microparticles

Cited by 5 publications

References 42 publications

The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation

The Adsorption of P2X2 Receptors Interacting with IgG Antibodies Revealed by Combined AFM Imaging and Mechanical Simulation

A Review of Transition Metal Dichalcogenides-Based Biosensors

Investigating Crystalline Protein Suspension Formulations of Pembrolizumab from MAS NMR Spectroscopy

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