scispace - formally typeset
Search or ask a question

What results were obtained studying antibody aggregation ? 


Best insight from top research papers

Antibody aggregation was studied in several papers. One study found that high concentration antibody solutions with rich multimers had a deeper color, indicating the presence of multimers. LC-MS analysis showed that the multimers had a complex structure and ICP-MS analysis revealed a higher concentration of iron ions in the multimers . Another study used in silico analysis to investigate antibody aggregation and found that the presence of glycans in the Fc region of antibodies influenced the aggregation prone regions (APR) of the antibodies . A third study investigated the effect of hydrodynamic flow and solid-liquid interfaces on protein aggregation and found that changes in the materials of the syringe barrels had a dramatic effect on protein aggregation, while increasing shear rate had a negligible effect . A fourth study used numerical simulations to study the hydrodynamic behavior of antibodies near silicone oil-water interfaces and found that protein loss from the bulk solution occurred as the molecules adsorbed at the interface . Finally, a study investigated the interaction of immunoglobulin G (IgG) antibodies with gold nanoparticles (AuNPs) and found that the addition of antibody triggered the aggregation of AuNPs at pH < 7.5, while a stable bioconjugate was formed at pH ≥ 7.5 .

Answers from top 5 papers

More filters
Papers (5)Insight
The results obtained from studying antibody aggregation showed that the addition of antibody triggered the aggregation of gold nanoparticles (AuNPs) at pH < 7.5, but a stable bioconjugate was formed at pH ≥ 7.5. The mechanism of aggregation was identified as electrostatic bridging between the antibody and the negatively charged AuNPs. The protein-AuNP interactions were reversible within the first few hours but became irreversible after 24 hours.
The study found that increasing shear rate had a negligible effect on protein aggregation, while changes in the materials of the syringe barrels had a dramatic effect on monomer loss.
The results obtained from studying antibody aggregation showed that the presence of glycans in the Fc region of antibodies can influence and potentially protect hydrophobic regions associated with aggregation. However, the size of the glycans may limit their influence on aggregation.
The results obtained from studying antibody aggregation include the observation of a deeper color in high concentration antibody solutions with rich multimers, as well as the identification of iron ions as an important factor in the formation of multimers.
The paper discusses the results of studying antibody aggregation near silicone oil-water interfaces, including protein loss from the bulk solution, dynamic cluster formation, and the effect of antibody concentration on diffusivity and aggregation propensity.

Related Questions

Why after fermentation, protein is aggregation?5 answersProtein aggregation after fermentation can occur due to various factors. During industrial production, proteins like monoclonal antibodies may aggregate at different stages, compromising their quality and efficacy. Proteins tend to aggregate, especially when stored at high concentrations, impacting stability and therapeutic properties. In the case of Lactobacillus brevis, aggregation is triggered by glucose fermentation, causing surface layer protein detachment and subsequent aggregation. Protein function relies on a defined 3D structure, with unfolding and aggregation affecting functionality. Recombinant proteins in genetically engineered organisms often form inclusion bodies due to aggregation, although recent studies suggest potential applications in various biotechnological fields. Overall, protein aggregation post-fermentation is a critical concern affecting protein stability, bioavailability, and therapeutic effectiveness.
What are the factors that influence protein aggregation?4 answersProtein aggregation is influenced by various factors. Physiological factors such as pH, temperature, salt, and pressure can impact protein structure and homeostasis. Environmental risk factors, such as pollutants, have also been found to play a role in protein aggregation disorders. Protein adsorption and desorption at the solid-liquid interface can lead to aggregation in prefilled syringes, with electrostatic interactions and hydrophobic effects being dominant forces. Different ways of protein aggregation include 3D domain swapping, salt bridge formation, and oxidative stress. Protein aggregation can be controlled during protein production, transport, and storage through various methods. Interactions between proteins and nanoplastics are influenced by electrostatic properties, protein structures, and solution chemistries, affecting aggregation kinetics. Overall, factors such as physiological conditions, environmental risk factors, protein adsorption, and solution chemistries can all influence protein aggregation.
What are the factors that affect the formation of aggregates?5 answersThe factors that affect the formation of aggregates include size-dependent diffusivity, rotational effects, settling under gravity, capillary pressure, interparticle attractive forces, charge heterogeneity, particle polarization, arbuscular mycorrhizal fungi (AMF), and pH value. Size-dependent diffusivity and rotational effects can slow down the growth rate of aggregates and decrease their fractal dimension. Capillary pressure can overwhelm repulsive electrostatic forces, leading to the assembly of aggregates that are out of thermal equilibrium. Charge heterogeneity and particle polarization can significantly alter the mechanical equilibrium of aggregates and hold particles together with electrostatic forces. AMF can influence the formation and stability of soil aggregates, with different AMF species having different effects. pH value can affect the morphology, physico-chemical properties, formation kinetics, and stability of amyloid and amyloid-like aggregates.
How does aggregation affect the shelf life of mAbs?5 answersAggregation of monoclonal antibodies (mAbs) can significantly impact their shelf life. Cryoconcentration during large-scale freezing can lead to regions of different ratios of low molecular weight excipients to protein, affecting mAb stability after frozen storage. The propensity for mAbs to aggregate at physiological and manufacturing pH values can prevent their use as therapeutic molecules or delay time to market. Aggregation of biotherapeutics is a major hindrance to the development of successful drug candidates, and rational design strategies can be employed to stabilize mAbs against aggregation. The fate of mAb and excipient particles can differ substantially depending on the nature of stress and the environment they are subjected to. Methods to predict the rates or propensities of protein aggregation are of great interest in biopharmaceutical research and development.
Are protein aggregates bigger than the proteins they are formed from?5 answersProtein aggregates can vary in size, ranging from nanometer aggregates (<100 nm) to sub-micron aggregates (100 nm - 1 μm) and micron aggregates (1 - 100 μm). The size of protein aggregates can be larger than the individual proteins they are formed from. For example, dimers comprising a large number of antibody molecules can have a diameter of up to 100 μm. Additionally, protein aggregates larger than hundreds of nanometers in diameter are difficult to physically fractionate. Therefore, protein aggregates can be significantly larger than the individual proteins they are formed from.
Can aggregates of proteins aggregate between them?4 answersProtein aggregates can aggregate between them. The ability of existing aggregates to replicate is a key property in generating their pathogenic effect. This suggests that aggregates can interact and form larger aggregates. Additionally, the effects of heat treatment and pH adjustment on whey protein aggregates indicate that these treatments can lead to the creation of aggregates with different sizes. These findings further support the idea that protein aggregates can aggregate between them.

See what other people are reading

What Fc mutations improve antibody half-lfe?
5 answers
What is the impact of flow pulsation on droplet deformation?
5 answers
What haptoglobin servers for?
4 answers
How do i model two viscous emulsion mixing in time ?
5 answers
What is the relationship between bacterial glycans and micro morphology?
5 answers
What is the relationship between bacterial glycans and micro morphology?
5 answers
What is shear thinning behaior?
5 answers
Shear thinning behavior refers to the phenomenon where a material's viscosity decreases under shear stress. This behavior is observed in various systems, such as particle suspensions and polymer hydrogels, and is influenced by factors like interparticle interactions, surface morphology, and molecular structure. In the case of particle suspensions, shear thinning can be controlled by frictional or adhesion forces between particles, leading to changes in rheological properties. For polymer hydrogels, shear-thinning properties can be achieved through the formation of supramolecular polymer nanofibers with hydrogen bonds, allowing for reversible gel formation and recovery under shear stress. Understanding the molecular origins of shear thinning is crucial for designing materials with tailored rheological properties for various applications.
What are the potential applications of glycosides in modulating protein function for therapeutic purposes?
5 answers
Glycans play a crucial role in modulating protein function for therapeutic purposes. They are involved in various processes such as protein folding, trafficking, receptor binding, and inflammation. Glycoengineering, which alters glycosylation patterns, is a promising strategy to enhance the properties of therapeutic proteins like erythropoietin and IgG monoclonal antibodies. Additionally, carbohydrates are essential for cellular communication, cancer modulation, and infection regulation, highlighting their significance in protein function modulation. Glycans, as carbohydrate-based polymers, are vital biomolecules with diverse effects, including anti-tumour, immune function, and anti-viral activities, showcasing their potential in therapeutic applications. Overall, glycosides offer a wide range of applications in modulating protein function for therapeutic benefits, making them valuable targets for drug development and clinical practice.
Why does a chlorinated glucose derivative with axial chlorines ring flip?
5 answers
The chlorinated glucose derivative undergoes ring flipping due to the presence of axial substituents, which induce conformational changes. Specifically, the axial-rich form of the pyranose ring, with bulky silyl-protecting groups on adjacent trans-diols, favors axial conformations, leading to ring flipping. This conformational change is crucial for achieving stereoselective glycosylation, as seen in the β-selective reaction induced by the axial-rich glucosyl donor. Additionally, the presence of axial chlorines in the molecule can lead to a shift from an amorphous to a crystalline form, driven by alkane-induced pore formation and weak interactions like phenolic OH···Cl hydrogen bonds. These interactions play a role in the reversible phase transition observed in the material.
How is the metabolism of N acetyl glucosamine in mammals?
5 answers
The metabolism of N-acetylglucosamine (GlcNAc) in mammals involves various pathways. GlcNAc can be converted to UDP-GlcNAc, which is crucial for glycan assembly in the Golgi apparatus. Additionally, GlcNAc can be metabolized to N-acetylneuraminic acid (Neu5Ac) and its hydroxylated derivative N-glycolylneuraminic acid (Neu5Gc). Interestingly, the hexosamine salvage pathway can convert N-glycolylglucosamine (GlcNGc) to UDP-GlcNGc, leading to the modification of proteins with O-GlcNGc. Furthermore, Neu5Gc can be incorporated into neural polysialic acid (polySia), where its resistance to sialidases prevents rapid turnover, potentially explaining the rarity of Neu5Gc in the vertebrate brain. Overall, the metabolism of GlcNAc in mammals involves intricate pathways that impact glycan assembly, protein modification, and neural development.
What role does clusterin play in regulating glucose homeostasis?
5 answers
Clusterin, a glycoprotein with diverse functions, plays a crucial role in regulating glucose homeostasis. Studies suggest that clusterin is involved in energy homeostasis, adipose tissue regulation, and insulin resistance. In high-fat diet-fed mice, clusterin knockout led to increased insulin resistance, higher glucose and C-peptide levels, and altered glucose uptake. Additionally, clusterin overexpression affected antioxidant, proteostatic, and metabolic pathways, impacting glucose levels and exacerbating diabetic phenotypes. These findings highlight clusterin's significance in modulating insulin sensitivity, oxidative stress, and inflammation, indicating its potential as a therapeutic target for managing conditions like diabetes and metabolic syndrome.