Forces between aqueous nonuniformly charged colloids from molecular simulation

Striolo, Alberto; Bratko, D.; Wu, Jianzhong; Elvassore, Nicola; Blanch, H.W.; Prausnitz, John M.

doi:10.1063/1.1467343

Cited by 52 publications

(38 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although the exact mechanism was hard to define, this complex mechanism with zeolite treatments might have resulted proteins to possess anisotropic charge distribution on their surfaces and this might have caused increase in dipoles. Thus protein-protein interactions might be attractive and lead aggregation to be energetically favorable [39,40].…”

Section: Characterization Resultsmentioning

confidence: 99%

Investigation of structural properties of clinoptilolite rich zeolites in simulated digestion conditions and their cytotoxicity against Caco-2 cells in vitro

Kavak

Ülkü

2012

J Porous Mater

View full text Add to dashboard Cite

The use of the clinoptilolite rich natural zeolites in biomedical applications such as in anticancer therapy, drug or drug support systems and as nutritive supplement is highly dependent on their behavior in digestive conditions. Aim of this study is to investigate structural stability of clinoptilolite rich natural zeolites in simulated digestion conditions and their interactions with digestive media and with Caco-2 (human colon adenocarcinoma) cells. X-ray Diffraction (XRD), Fourier Transform InfraRed (FTIR), Scanning Electron Microscopy (SEM) and Inductively Coupled Plasma Atomic Emission Spectroscopy (ICP-AES) analyses of the clinoptilolite rich zeolite samples showed that zeolites preserved their structural stabilities during in vitro digestion. Slight interactions were detected in UV measurements of the digestive liquid media and FTIR spectra of the intestinal digested media powders. SEM results implied that zeolites might have a role in the aggregation of the digestive enzymes. Cytotoxicity test using colon cancer cells showed that clinoptilolite rich natural zeolites have cytotoxic effect against Caco-2 cells and cytotoxicity did not significantly change with respect to simulated digestion process.

show abstract

Section: Characterization Resultsmentioning

confidence: 99%

Investigation of structural properties of clinoptilolite rich zeolites in simulated digestion conditions and their cytotoxicity against Caco-2 cells in vitro

Kavak

Ülkü

2012

J Porous Mater

View full text Add to dashboard Cite

show abstract

“…In such cases, protein-protein interactions are frequent, making assembly processes such as aggregation energetically favorable (Striolo et al, 2002).…”

Section: Exposure To Ph Conditions Near Protein Isoelectric Pointmentioning

confidence: 99%

Aggregates in monoclonal antibody manufacturing processes

Vázquez-Rey¹,

Lang

2011

Biotech & Bioengineering

417

304

View full text Add to dashboard Cite

Monoclonal antibodies have proved to be a highly successful class of therapeutic products. Large-scale manufacturing of pharmaceutical antibodies is a complex activity that requires considerable effort in both process and analytical development. If a therapeutic protein cannot be stabilized adequately, it will lose partially or totally its therapeutic properties or even cause immunogenic reactions thus potentially further endangering the patients' health. The phenomenon of protein aggregation is a common issue that compromises the quality, safety, and efficacy of antibodies and can happen at different steps of the manufacturing process, including fermentation, purification, final formulation, and storage. Aggregate levels in drug substance and final drug product are a key factor when assessing quality attributes of the molecule, since aggregation might impact biological activity of the biopharmaceutical. In this review it is analyzed how aggregates are formed during monoclonal antibody industrial production, why they have to be removed and the manufacturing process steps that are designed to either minimize or remove aggregates in the final product.

show abstract

“…The DLVO potential has been successfully applied to many colloidal systems and protein solutions [3,4]. However, it does not seem to fully explain the rich behaviour of proteins [4,7,8,9], and due to the complexity of these systems (anisotropic property, irregular shape, distributed charge patches, etc. ), a complete understanding of the properties of the effective interactions between protein molecules in solutions remains a challenge [8].…”

mentioning

confidence: 99%

Effective Long-Range Attraction between Protein Molecules in Solutions Studied by Small Angle Neutron Scattering

et al. 2005

View full text Add to dashboard Cite

Small angle neutron scattering intensity distributions taken from cytochrome C and lysozyme protein solutions show a rising intensity at very small wave vector, Q, which can be interpreted in terms of the presence of a weak long-range attraction between protein molecules. This interaction has a range several times that of the diameter of the protein molecule, much greater than the range of the screened electrostatic repulsion. We show evidence that this long-range attraction is closely related to the type of anion present and ion concentration in the solution.PACS numbers: 87.14. Ee,61.12.Ex, 82.35.Rs The bottleneck of protein crystallography is the lack of systematic methods to obtain protein crystals. This is partly due to incomplete understanding of the physical chemistry conditions controlling the growth of protein crystals. A full comprehension of the effective protein interactions and phase behavior is therefore essential. It has been shown that the crystallization curves of some globular proteins appear to coincide with the phase diagrams of a hard sphere system interacting with a short range attraction [1,2,3]. Small angle neutron and X-ray scattering investigations of proteins suggest the presence of a short-range attractive interaction between protein molecules besides the electrostatic repulsion induced by the residual charges [4,5,6]. The DLVO potential has been successfully applied to many colloidal systems and protein solutions [3,4]. However, it does not seem to fully explain the rich behaviour of proteins [4,7,8,9], and due to the complexity of these systems (anisotropic property, irregular shape, distributed charge patches, etc.), a complete understanding of the properties of the effective interactions between protein molecules in solutions remains a challenge [8].Recent measurements of small angle neutron scattering (SANS) intensity distribution in protein solutions show interesting results [5,6,10]. Beside the normal first diffraction peak, it is present a peak (cluster peak) appearing at a much smaller scattering wave vector, Q, due to the formation of ordered clusters. The appearance of a cluster peak is explained as due to the competition of a short-range attraction and a long-range electrostatic repulsion [5,11,12]. Moreover, a rising intensity as Q approaches zero (zero-Q peak) is observed in both liquid-like and solid-like samples, which implies that the effective potential should have more features in addition to the well known short-range attraction and electrostatic repulsion. The existence of a long-range attraction between protein molecules has already been

show abstract

Forces between aqueous nonuniformly charged colloids from molecular simulation

Cited by 52 publications

References 42 publications

Investigation of structural properties of clinoptilolite rich zeolites in simulated digestion conditions and their cytotoxicity against Caco-2 cells in vitro

Investigation of structural properties of clinoptilolite rich zeolites in simulated digestion conditions and their cytotoxicity against Caco-2 cells in vitro

Aggregates in monoclonal antibody manufacturing processes

Effective Long-Range Attraction between Protein Molecules in Solutions Studied by Small Angle Neutron Scattering

Contact Info

Product

Resources

About