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Highly Concentrated Monoclonal Antibody Solutions: Direct Analysis of Physical Structure and Thermal Stability
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Examination of the secondary structure of proteins by deconvolved FTIR spectra
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Derivative Absorbance Spectroscopy and Protein Phase Diagrams as Tools for Comprehensive Protein Characterization: A bGCSF Case Study
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Challenges in the development of high protein concentration formulations
inferredcites →https://doi.org/10.1002/jps.20178openalex-snapshot
Antibody Pharmacokinetics and Pharmacodynamics
inferredcites →https://doi.org/10.1002/jps.20342openalex-snapshot
Application of Ultrasonic Shear Rheometer to Characterize Rheological Properties of High Protein Concentration Solutions at Microliter Volume
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Reversible Self-Association Increases the Viscosity of a Concentrated Monoclonal Antibody in Aqueous Solution
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Solution Behavior of IFN-β-1a: An Empirical Phase Diagram Based Approach
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Influence of macromolecular crowding upon the stability and state of association of proteins: Predictions and observations
inferredcites →https://doi.org/10.1007/978-0-387-76643-0_9openalex-snapshot
Challenges in the Development of High Protein Concentration Formulations
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Principles of Fluorescence Spectroscopy
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Front-face fluorometry of liquid samples
inferredcites →https://doi.org/10.1016/0005-2795(81)90103-3openalex-snapshot
Evidence for protein self-association induced by excluded volume Myoglobin in the presence of globular proteins
inferredcites →https://doi.org/10.1016/s0006-3495(00)76602-1openalex-snapshot
The Thermal Stability of Immunoglobulin: Unfolding and Aggregation of a Multi-Domain Protein
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Myoglobin and hemoglobin rotational diffusion in the cell
inferredcites →https://doi.org/10.1016/s0021-9258(17)37926-7openalex-snapshot
Determination of the apparent thermodynamic activities of saturated protein solutions.
inferredcites →https://doi.org/10.1016/s0021-9258(19)38653-3openalex-snapshot
Comparison of the biophysical characteristics of human brain-derived neurotrophic factor, neurotrophin-3, and nerve growth factor
inferredcites →https://doi.org/10.1016/s0022-2836(02)01443-2openalex-snapshot
Effect of Dextran on Protein Stability and Conformation Attributed to Macromolecular Crowding
inferredcites →https://doi.org/10.1016/s0022-2836(77)80191-5openalex-snapshot
Analysis of non-ideal behavior in concentrated hemoglobin solutions
inferredcites →https://doi.org/10.1016/s0959-440x(99)00045-7openalex-snapshot
Implications of macromolecular crowding for protein assembly
inferredcites →https://doi.org/10.1016/s0968-0004(01)01938-7openalex-snapshot
Macromolecular crowding: obvious but underappreciated
inferredcites →https://doi.org/10.1021/bi00033a024openalex-snapshot
Temperature-Induced Changes in Protein Structures Studied by Fourier Transform Infrared Spectroscopy and Global Analysis
inferredcites →https://doi.org/10.1021/bi00091a036openalex-snapshot
Refolding of brain-derived neurotrophic factor from guanidine hydrochloride: Kinetic trapping in a collapsed form which is incompetent for dimerization
inferredcites →https://doi.org/10.1021/bi00133a007openalex-snapshot
Dimeric structure and conformational stability of brain-derived neurotrophic factor and neurotrophin-3
inferredcites →https://doi.org/10.1023/b:pham.0000032993.98705.73openalex-snapshot
Opalescent Appearance of an IgG1 Antibody at High Concentrations and Its Relationship to Noncovalent Association
inferredcites →https://doi.org/10.1074/jbc.r100005200openalex-snapshot
The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media
inferredcites →https://doi.org/10.1110/ps.03288104openalex-snapshot
Protein folding by the effects of macromolecular crowding
inferredcites →https://doi.org/10.1110/ps.051678205openalex-snapshot
Undistorted structural analysis of soluble proteins by attenuated total reflectance infrared spectroscopy
inferredcites →https://doi.org/10.1146/annurev.bb.22.060193.000331openalex-snapshot
Macromolecular Crowding: Biochemical, Biophysical, and Physiological Consequences
inferredcites →https://doi.org/10.1208/ps050210openalex-snapshot
Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Extrapolating Differential Scanning Calorimetry Data for Monoclonal Antibodies to Low Temperatures
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Process Development of Protein Therapeutics
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Process Development of Protein Therapeutics
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Proteins: Thermal Unfolding
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Antibody Expression in Mammalian Cells
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The Formulation and Delivery of Monoclonal Antibodies
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Manufacturing Specialties
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Analytical Characterization of Proteins and Peptides
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Development of Formulations for Therapeutic Monoclonal Antibodies and Fc Fusion Proteins
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Physical Stability of Protein Pharmaceuticals
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An Empirical Phase Diagram–High‐Throughput Screening Approach to the Characterization and Formulation of Biopharmaceuticals
inferred← citeshttps://doi.org/10.1002/9780470769829.ch4openalex-snapshot
External Factors Affecting Protein Aggregation
inferred← citeshttps://doi.org/10.1002/9781118150573.ch10openalex-snapshot
Infrared Spectroscopy to Characterize Protein Aggregates
inferred← citeshttps://doi.org/10.1002/9781118150573.ch8openalex-snapshot
Ultraviolet Absorption Spectroscopy
inferred← citeshttps://doi.org/10.1002/9781118354698.ch3openalex-snapshot
Solubility and Early Assessment of Stability for Protein Therapeutics
inferred← citeshttps://doi.org/10.1002/9781118354698.ch4openalex-snapshot
Biophysical and Structural Characterization Needed Prior to Proof of Concept
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Nucleation, Aggregation, and Conformational Distortion
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Stabilization and Formulation of Vaccines
inferred← citeshttps://doi.org/10.1002/9783527682423.ch8openalex-snapshot
Glycosylation of Antibody Molecules
inferred← citeshttps://doi.org/10.1002/biot.200800274openalex-snapshot
Lysozyme‐lysozyme self‐interactions as assessed by the osmotic second virial coefficient: Impact for physical protein stabilization
inferred← citeshttps://doi.org/10.1002/biot.201400052openalex-snapshot
Avoiding antibody aggregation during processing: Establishing hold times
inferred← citeshttps://doi.org/10.1002/btpr.2464openalex-snapshot
Differential scanning calorimetry and fluorimetry measurements of monoclonal antibodies and reference proteins: Effect of scanning rate and dye selection
inferred← citeshttps://doi.org/10.1002/jps.20964openalex-snapshot
The effective hard particle model provides a simple, robust, and broadly applicable description of nonideal behavior in concentrated solutions of bovine serum albumin and other nonassociating proteins
inferred← citeshttps://doi.org/10.1002/jps.21327openalex-snapshot
Measuring and Increasing Protein Solubility
inferred← citeshttps://doi.org/10.1002/jps.21610openalex-snapshot
Viscoelastic characterization of high concentration antibody formulations using quartz crystal microbalance with dissipation monitoring
inferred← citeshttps://doi.org/10.1002/jps.21617openalex-snapshot
Characterization of the photodegradation of a human IgG1 monoclonal antibody formulated as a high-concentration liquid dosage form
inferred← citeshttps://doi.org/10.1002/jps.21768openalex-snapshot
Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation, and accelerated stress studies
inferred← citeshttps://doi.org/10.1002/jps.21778openalex-snapshot
Tungsten-induced protein aggregation: Solution behavior
inferred← citeshttps://doi.org/10.1002/jps.21938openalex-snapshot
Use of a folding model and in situ spectroscopic techniques for rational formulation development and stability testing of monoclonal antibody therapeutics**Gauri Rao and Vandana Iyer contributed equally to this work.
inferred← citeshttps://doi.org/10.1002/jps.21955openalex-snapshot
High throughput thermostability screening of monoclonal antibody formulations
inferred← citeshttps://doi.org/10.1002/jps.22036openalex-snapshot
Detection of IgG Aggregation by a High Throughput Method Based on Extrinsic Fluorescence
inferred← citeshttps://doi.org/10.1002/jps.22190openalex-snapshot
Factors Affecting the Viscosity in High Concentration Solutions of Different Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1002/jps.22401openalex-snapshot
Noncovalent Pegylation by Dansyl-Poly(ethylene Glycol)s as a New Means Against Aggregation of Salmon Calcitonin
inferred← citeshttps://doi.org/10.1002/jps.22618openalex-snapshot
Multidimensional methods for the formulation of biopharmaceuticals and vaccines
inferred← citeshttps://doi.org/10.1002/jps.22650openalex-snapshot
Opalescence of an IgG2 monoclonal antibody solution as it relates to liquid–liquid phase separation
inferred← citeshttps://doi.org/10.1002/jps.22712openalex-snapshot
High‐Throughput Assessment of Thermal and Colloidal Stability Parameters for Monoclonal Antibody Formulations
inferred← citeshttps://doi.org/10.1002/jps.23008openalex-snapshot
Formulation Design and High-Throughput Excipient Selection Based on Structural Integrity and Conformational Stability of Dilute and Highly Concentrated IgG1 Monoclonal Antibody Solutions
inferred← citeshttps://doi.org/10.1002/jps.23076openalex-snapshot
Comparison of High-Throughput Biophysical Methods to Identify Stabilizing Excipients for a Model IgG2 Monoclonal Antibody: Conformational Stability and Kinetic Aggregation Measurements
inferred← citeshttps://doi.org/10.1002/jps.23187openalex-snapshot
Excipients Differentially Influence the Conformational Stability and Pretransition Dynamics of Two IgG1 Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1002/jps.23188openalex-snapshot
An Application of Ultraviolet Spectroscopy to Study Interactions in Proteins Solutions at High Concentrations
inferred← citeshttps://doi.org/10.1002/jps.23256openalex-snapshot
Antibody nanoparticle dispersions formed with mixtures of crowding molecules retain activity and In Vivo bioavailability
inferred← citeshttps://doi.org/10.1002/jps.23367openalex-snapshot
Comparative Signature Diagrams to Evaluate Biophysical Data for Differences in Protein Structure Across Various Formulations
inferred← citeshttps://doi.org/10.1002/jps.23633openalex-snapshot
DSF Method Optimization and Its Application in Predicting Protein Thermal Aggregation Kinetics
inferred← citeshttps://doi.org/10.1002/jps.23748openalex-snapshot
Linking the Solution Viscosity of an IgG2 Monoclonal Antibody to Its Structure as a Function of pH and Temperature
inferred← citeshttps://doi.org/10.1002/jps.24240openalex-snapshot
Optimized UV Detection of High-Concentration Antibody Formulations using High-Throughput SE-HPLC
inferred← citeshttps://doi.org/10.1002/jps.24408openalex-snapshot
Application of a High-Throughput Relative Chemical Stability Assay to Screen Therapeutic Protein Formulations by Assessment of Conformational Stability and Correlation to Aggregation Propensity
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Advanced analyses of kinetic stabilities of iggs modified by mutations and glycosylation
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Aggregation of a multidomain protein: A coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress
inferred← citeshttps://doi.org/10.1002/pro.3278openalex-snapshot
Analysis of IgG kinetic stability by differential scanning calorimetry, probe fluorescence and light scattering
inferred← citeshttps://doi.org/10.1002/prot.25354openalex-snapshot
Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry
inferred← citeshttps://doi.org/10.1007/978-1-4614-4316-2_2openalex-snapshot
High-Throughput Biophysical Approaches to Therapeutic Protein Development
inferred← citeshttps://doi.org/10.1007/978-1-4939-9678-0_9openalex-snapshot
Differential Scanning Calorimetry to Quantify Heat-Induced Aggregation in Concentrated Protein Solutions
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Chapter 7: An Empirical Phase Diagram: High-Throughput Screening Approach to the Characterization and Formulation of Biopharmaceuticals
inferred← citeshttps://doi.org/10.1007/978-3-030-31415-6_8openalex-snapshot
Chapter 8: Biophysical Characterization and the Development of Therapeutic Proteins
inferred← citeshttps://doi.org/10.1007/978-3-319-90603-4_4openalex-snapshot
Introduction to High-Concentration Proteins
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The effect of formulation variables on protein stability and integrity of a model IgG4 monoclonal antibody and translation to formulation of a model ScFv
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Thermal Unfolding Curves of High Concentration Bovine IgG Measured by FTIR Spectroscopy
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Behavior of Monoclonal Antibodies: Relation Between the Second Virial Coefficient (B 2) at Low Concentrations and Aggregation Propensity and Viscosity at High Concentrations
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Effects of Ionic Strength and Sugars on the Aggregation Propensity of Monoclonal Antibodies: Influence of Colloidal and Conformational Stabilities
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Concentration Dependent Viscosity of Monoclonal Antibody Solutions: Explaining Experimental Behavior in Terms of Molecular Properties
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Expanding the toolbox for predictive parameters describing antibody stability considering thermodynamic and kinetic determinants
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Evaluation of Ion Mobility-Mass Spectrometry for Comparative Analysis of Monoclonal Antibodies
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Aggregation, stability, and formulation of human antibody therapeutics
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Stability analysis of monoclonal antibodies
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Differential Scanning Calorimetry in the Biopharmaceutical Sciences
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Differential scanning calorimetry in the biopharmaceutical sciences
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Analysis of high-throughput data
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Online fluorescent dye detection method for the characterization of immunoglobulin G aggregation by size exclusion chromatography and asymmetrical flow field flow fractionation
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Concomitant Raman spectroscopy and dynamic light scattering for characterization of therapeutic proteins at high concentrations
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A methodological approach for the thermal stability and stress exposure studies of a model antibody
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Reversibility and irreversibility in the temperature denaturation of monoclonal antibodies
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Extrapolating differential scanning calorimetry data for monoclonal antibodies to low temperatures
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Protein–excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development
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Chemical degradation of proteins in the solid state with a focus on photochemical reactions
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Challenges and developments in the manufacturing of high-concentration biotherapeutic monoclonal antibodies
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Quantitative NMR study of heat-induced aggregation of eye-lens crystallin proteins under crowding conditions
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Characterization of recombinant antibodies for cancer therapy by infrared spectroscopy
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High-Throughput Analysis of Concentration-Dependent Antibody Self-Association
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Unfolding and aggregation of monoclonal antibodies on cation exchange columns: Effects of resin type, load buffer, and protein stability
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A critical evaluation of self-interaction chromatography as a predictive tool for the assessment of protein–protein interactions in protein formulation development: A case study of a therapeutic monoclonal antibody
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Biophysical stability of hyFc fusion protein with regards to buffers and various excipients
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Effects of annealing on the physical properties of therapeutic proteins during freeze drying process
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Feasibility of circular dichroism to study protein structure at extreme concentrations
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Amyloidogenic and non-amyloidogenic molten globule conformation of β-lactoglobulin in self-crowded regime
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Comparison of different protein concentration techniques within preformulation development
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Long-term stability of diluted solutions of the monoclonal antibody rituximab
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Differential scanning fluorescence approach using a fluorescent molecular rotor to detect thermostability of proteins in surfactant-containing formulations
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Long-term physico-chemical stability of diluted trastuzumab
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Prediction and characterization of the stability enhancing effect of the Cherry-Tag™ in highly concentrated protein solutions by complex rheological measurements and MD simulations
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Science and art of protein formulation development
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Aggregation of therapeutic monoclonal antibodies due to thermal and air/liquid interfacial agitation stress: Occurrence, stability assessment strategies, aggregation mechanism, influencing factors, and ways to enhance stability
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Impact of electroviscous effect on viscosity in developing highly concentrated protein formulations: Lessons from non-protein charged colloids
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Interactions between immunoglobulin G molecules
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Arginine and lysine reduce the high viscosity of serum albumin solutions for pharmaceutical injection
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Three spectroscopic techniques evaluated as a tool to study the effects of iodination of monoclonal antibodies, exemplified by rituximab
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Long-term stability of bevacizumab repackaged in 1 mL polypropylene syringes for intravitreal administration
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One-month stability study of a biosimilar of infliximab (Remsima®) after dilution and storage at 4 °C and 25 °C
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Extended stability of the rituximab biosimilar CT-P10 in its opened vials and after dilution and storage in polyolefin bags
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Separation of recombinant monoclonal antibodies IgG201 from a cell culture supernatant using an integrated aqueous two-phase system with thermo-separating EOPO
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Immunosignaturing: a critical review
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Relating Protein–Protein Interactions and Aggregation Rates From Low to High Concentrations
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How Well Do Low- and High-Concentration Protein Interactions Predict Solution Viscosities of Monoclonal Antibodies?
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Physicochemical Stability of Monoclonal Antibodies: A Review
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Effect of Linker-Drug Properties and Conjugation Site on the Physical Stability of ADCs
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Evaluation of a Raman Chemometric Method for Detecting Protein Structural Conformational Changes in Solution
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Synergistic Effects of Multiple Excipients on Controlling Viscosity of Concentrated Protein Dispersions
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Reformulation and Thermal Stability of a Therapeutic Anti-Cocaine mAb
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Folding Considerations for Therapeutic Protein Formulations
inferred← citeshttps://doi.org/10.1021/acs.biomac.0c01652openalex-snapshot
Amyloid Self-Assembly of Lysozyme in Self-Crowded Conditions: The Formation of a Protein Oligomer Hydrogel
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.1c00043openalex-snapshot
Visible Light Degradation of a Monoclonal Antibody in a High-Concentration Formulation: Characterization of a Tryptophan-Derived Chromophoric Photo-product by Comparison to Photo-degradation of N-Acetyl- l -tryptophan Amide
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Spray-Dried Monoclonal Antibody Suspension for High-Concentration and Low-Viscosity Subcutaneous Injection
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Silylated Precision Particles for Controlled Release of Proteins
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Quantitative Characterization of Weak Self-Association in Concentrated Solutions of Immunoglobulin G via the Measurement of Sedimentation Equilibrium and Osmotic Pressure
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Hard Quasispherical Particle Models for the Viscosity of Solutions of Protein Mixtures
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Increasing IgG Concentration Modulates the Conformational Heterogeneity and Bonding Network that Influence Solution Properties
inferred← citeshttps://doi.org/10.1021/la9023426openalex-snapshot
Low Viscosity Highly Concentrated Injectable Nonaqueous Suspensions of Lysozyme Microparticles
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Advancements in High Throughput Biophysical Technologies: Applications for Characterization and Screening during Early Formulation Development of Monoclonal Antibodies
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Solution pH That Minimizes Self-Association of Three Monoclonal Antibodies Is Strongly Dependent on Ionic Strength
inferred← citeshttps://doi.org/10.1021/mp400666bopenalex-snapshot
Examination of Thermal Unfolding and Aggregation Profiles of a Series of Developable Therapeutic Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1021/mp5000218openalex-snapshot
Specific Decrease in Solution Viscosity of Antibodies by Arginine for Therapeutic Formulations
inferred← citeshttps://doi.org/10.1021/mp900110qopenalex-snapshot
Biophysical and Stabilization Studies of the Chlamydia trachomatis Mouse Pneumonitis Major Outer Membrane Protein
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Stability testing in monoclonal antibodies
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Comparing domain interactions within antibody Fabs with kappa and lambda light chains
inferred← citeshttps://doi.org/10.1093/protein/gzv045openalex-snapshot
Discovery of highly soluble antibodies prior to purification using affinity-capture self-interaction nanoparticle spectroscopy
inferred← citeshttps://doi.org/10.1111/jphp.12621openalex-snapshot
Low-volume solubility assessment during high-concentration protein formulation development
inferred← citeshttps://doi.org/10.1146/annurev-chembioeng-062011-081052openalex-snapshot
Engineering Aggregation-Resistant Antibodies
inferred← citeshttps://doi.org/10.1177/1087057114557781openalex-snapshot
High-Throughput Screening of Formulations to Optimize the Thermal Stability of a Therapeutic Monoclonal Antibody
inferred← citeshttps://doi.org/10.1177/1087057114565593openalex-snapshot
Accelerated Formulation Development of Monoclonal Antibodies (mAbs) and mAb-Based Modalities: Review of Methods and Tools
inferred← citeshttps://doi.org/10.1177/2472630318780620openalex-snapshot
Improved Fluorescence Methods for High-Throughput Protein Formulation Screening
inferred← citeshttps://doi.org/10.1515/pthp-2022-0007openalex-snapshot
Physicochemical stability study of a biosimilar of Bevacizumab in vials and after dilution in 0.9% NaCl in polyolefin intravenous bags
inferred← citeshttps://doi.org/10.1533/9781908818102.13openalex-snapshot
A formulation method to improve the physical stability of macromolecular-based drug products
inferred← citeshttps://doi.org/10.18130/v34g8dopenalex-snapshot
Unfolding and Aggregation of Monoclonal Antibodies during Cation Exchange Chromoatography
inferred← citeshttps://doi.org/10.2174/1570163819666220624092622openalex-snapshot
Physical Instabilities of Therapeutic Monoclonal Antibodies: A Critical Review
inferred← citeshttps://doi.org/10.3233/hab-2009-0211openalex-snapshot
The preparation of radiolabeled monoclonal antibodies for human use
inferred← citeshttps://doi.org/10.3389/fimmu.2017.01860openalex-snapshot
Engineering of Fc Fragments with Optimized Physicochemical Properties Implying Improvement of Clinical Potentials for Fc-Based Therapeutics
inferred← citeshttps://doi.org/10.3390/antib7030024openalex-snapshot
Engaging with Raman Spectroscopy to Investigate Antibody Aggregation
inferred← citeshttps://doi.org/10.3390/antib9020008openalex-snapshot
Fast Confirmation of Antibody Identity by MALDI-TOF MS Fingerprints
inferred← citeshttps://doi.org/10.3390/molecules191220888openalex-snapshot
Combined Dynamic Light Scattering and Raman Spectroscopy Approach for Characterizing the Aggregation of Therapeutic Proteins
inferred← citeshttps://doi.org/10.3390/pharmaceutics10040165openalex-snapshot
An Evaluation of the Potential of NMR Spectroscopy and Computational Modelling Methods to Inform Biopharmaceutical Formulations
inferred← citeshttps://doi.org/10.3390/pharmaceutics13040534openalex-snapshot
Analytical Techniques for Structural Characterization of Proteins in Solid Pharmaceutical Forms: An Overview
inferred← citeshttps://doi.org/10.4161/hv.25788openalex-snapshot
Biophysical and formulation studies of theSchistosoma mansoniTSP-2 extracellular domain recombinant protein, a lead vaccine candidate antigen for intestinal schistosomiasis
inferred← citeshttps://doi.org/10.4161/mabs.19869openalex-snapshot
Solubility evaluation of murine hybridoma antibodies
inferred← citeshttps://doi.org/10.51847/ezjq1qe89aopenalex-snapshot
Comparative biosimilar quality studies between a rituximab product and MabThera
inferred← citeshttps://doi.org/10.5282/edoc.17520openalex-snapshot
Temperature-induced unfolding, aggregation, and interaction of therapeutic monoclonal antibodies
inferred← citeshttps://doi.org/10.5451/unibas-004655727openalex-snapshot
Impact of filling processes on protein solutions
inferred← citeshttps://doi.org/10.58088/3rnn-ad06openalex-snapshot
Molecular-scale understanding of protein interactions and solution viscosities
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