scholarly journals Potential and limits of a colloid approach to protein solutions

Soft Matter ◽  
2020 ◽  
Vol 16 (2) ◽  
pp. 307-323 ◽  
Author(s):  
Anna Stradner ◽  
Peter Schurtenberger

We critically discuss the application of colloid science concepts to better understand protein solution properties in the entire concentration range.

Antibodies ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 21
Author(s):  
Alexandre Ambrogelly

The color of a therapeutic monoclonal antibody solution is a critical quality attribute. Consistency of color is typically assessed at time of release and during stability studies against preset criteria for late stage clinical and commercial products. A therapeutic protein solution’s color may be determined by visual inspection or by more quantitative methods as per the different geographical area compendia. The nature and intensity of the color of a therapeutic protein solution is typically determined relative to calibrated standards. This review covers the analytical methodologies used for determining the color of a protein solution and presents an overview of protein variants and impurities known to contribute to colored recombinant therapeutic protein solutions.


2009 ◽  
Vol 2009 ◽  
pp. 1-5 ◽  
Author(s):  
Raymond Maikokera ◽  
Habauka M. Kwaambwa

The intrinsic viscosity of the coagulant protein was evaluated from the flow times of the protein solutions through a capillary viscometer, and the results suggested the coagulant protein to be globular. The interactions of the coagulant protein with anionic surfactant sodium dodecyl sulphate (SDS) and sodium dodecyl benzene sulfonate (SDBS) were also investigated by capillary viscometry. We conclude that there is strong protein-surfactant interaction at very low surfactant concentrations, and the behavior of the anionic surfactants in solutions containing coagulant protein is very similar. The viscometry results of protein-SDS system are compared with surface tension, fluorescence, and circular dichroism reported earlier. Combining the results of the four studies, the four approaches seem to confirm the same picture of the coagulant protein-SDS interaction. All the physical quantities when studied as function of surfactant concentration for 0.05% (w/v) protein solution either exhibited a maximum or minimum at a critical SDS concentration.


1922 ◽  
Vol 4 (5) ◽  
pp. 617-619 ◽  
Author(s):  
Jacques Loeb

1. It had been noticed in the previous experiments on the influence of the hydrogen ion concentration on the P.D. between protein solutions inside a collodion bag and aqueous solutions free from protein that the agreement between the observed values and the values calculated on the basis of Donnan's theory was not satisfactory near the isoelectric point of the protein solution. It was suspected that this was due to the uncertainty in the measurements of the pH of the outside aqueous solution near the isoelectric point. This turned out to be correct, since it is shown in this paper that the discrepancy disappears when both the inside and outside solutions contain a buffer salt. 2. This removes the last discrepancy between the observed P.D. and the P. D. calculated on the basis of Donnan's theory of P.D. between membrane equilibria, so that we can state that the P.D. between protein solutions inside collodion bags and outside aqueous solutions free from protein can be calculated from differences in the hydrogen ion concentration on the opposite sides of the membrane, in agreement with Donnan's formula.


Author(s):  
Dejuan Kong ◽  
Anita Penkova ◽  
Satwindar Singh Sadhal

Protein aggregation rate is known to be influenced by shear flow in protein solutions. This has important physiological implications as many of the body functions involve shear flow. Fluid mechanical shear can affect interactions between protein molecules, initiate protein aggregation, and further affect their biological activity. The shear rate is therefore an important parameter either to determine or to influence the properties of the protein solution when it forms a nucleus or aggregates. For experiments, the number density of nuclei can be controlled by using an optimal shear rate and protein concentration. However, this requires theoretical information on the shear rate for the experimental conditions. With this motivation, we have designed an experiment in which we can effectively apply shear with flow characteristics that can be calculated. Specifically, in a small hemispherically-shaped bowl, 4 mm in diameter we place the protein solution and insert a rounded rod that can be vibrated rotationally or laterally, maintaining spherical symmetry in the liquid region. This system is particularly useful when only small quantities of expensive protein solutions can be used for experimentation. We have carried out the mathematical analysis of the time-dependent flow field between two concentric hemispheres by the perturbation method using ε = U0/ωa ≪ 1 as a small parameter where U0 is a characteristic velocity, ω is the oscillation frequency and a is a length scale based on the vessel dimensions (bowl radius). We have obtained an analytical solution for the velocity field, and the shear rate in the liquid. In addition, with the nonlinear interaction of the oscillatory flow, there is a nonzero time-independent mean flow (known as streaming). With the integrated effect of shear in the liquid region, this result will be useful for conducting aggregation experiment in which the effective shear rate can be correlated to the aggregation rate.


2002 ◽  
Vol 16 (01n02) ◽  
pp. 354-358 ◽  
Author(s):  
PUI SHAN CHOW ◽  
JING ZHANG ◽  
XIANG YANG LIU ◽  
REGINALD BENG HEE TAN

Lysozyme was chosen as a model system for investigation of spherulitic growth in protein solution. Solutions of various concentrations of lysozyme and sodium chloride were studied under an optical microscope using polarized light. Spherulites were observed in the liquid-liquid separation regime. Images at various stages during the crystal growth process are presented. In a separate set of experiments, it was demonstrated that the presence of foreign particles could promote spherulitic growth even without liquid-liquid separation.


2018 ◽  
Vol 561-562 ◽  
pp. 70-88 ◽  
Author(s):  
Jacob Blaffert ◽  
Haleh Hashemi Haeri ◽  
Michaela Blech ◽  
Dariush Hinderberger ◽  
Patrick Garidel

2000 ◽  
Author(s):  
F. G. Tseng ◽  
H. M. Huang ◽  
C. S. Liu ◽  
C. Y. Huang ◽  
S. C. Lin ◽  
...  

Abstract A novel protein arraying method is proposed by utilizing micro stamps to spot proteins on a bio-absorption surface. The method can pick up various protein solutions to spot onto a desired substrate for protein immobilization. The fabrication process of the micro stamp combines surface micromachining and molding process. Successful transfer of BSA protein solution onto a PVDF (Polyvinylidene difluoride) surface has been demonstrated by using the micro fabricated stamps. The size of stamped protein spot in this stage is about 20–50% larger than that of the stamp. To quickly verify the protein binding ability to two different substrates: PVDF and PhastGel® Pad, a chopstick system is used to pickup protein solution for stamping. Result shows that appreciable amount protein retention is achieved for at least 6 hours on both substrates. Improved spotting size and position control on micro stamping process has also been carried out by stamp surface coating with aluminum/aluminum oxide and stamp picking up protein-solutions from a protein-solution pre-wetted clean room tissue.


J. Loeb, in a recent and stimulating work (1), has given a convincing, if somewhat over-emphatic, study of the colloidal behaviour of proteins in solution, based largely upon the theory of the Membrane Equilibrium first suggested by Donnan (4). In one important particular, however, his argument is incorrect. Loeb observed, by certain means (2) devised by himself, the potential difference (P. D.) between a protein solution on one side of a semipermeable membrane and a solution of acid, or of acid and salt, on the other side. He found this P. D. to vary as the concentration of hydrogen ions, or of salt, was varied, in the same manner as did a number of other factors (osmotic pressure, viscosity and swelling). He found also that this P. D. could be “calculated” from the observed difference of ρ -H (or of ρ -Cl) in the two solutions, on the basis of the theory of the Donnan Equilibrium, and he concludes that the excellent agreement between calculated and observed is a strong argument in favour of his explanation of other colloidal phenomena by that theory. This conclusion is not correct: the equality found by Loeb of the observed P. D., to that calculated from the difference of ρ -H is a necessary consequence of any mechanism which does not offend the Second Law of Thermodynamics, and in itself offers no support to the theory that the Donnan Equilibrium underlies the colloidal behaviour of protein solutions. That theory may rest on other and stronger ground; since, however, Loeb appears, throughout his book (and especially in Chapters VIII and IX) and in other places (2), (3), to lay great emphasis on this agreement of the observed P. D. with that “calculated” from the observed ρ -H’s it is necessary to point out that this agreement proves no more than that the system investigated was in equilibrium, and that the observations were accurately made.


1921 ◽  
Vol 4 (1) ◽  
pp. 97-112 ◽  
Author(s):  
Jacques Loeb

1. These experiments confirm the conclusion that protein solutions are true solutions consisting of isolated ions and molecules, and that these solutions may or may not contain in addition solid submicroscopic particles capable of occluding water. 2. The typical influence of electrolytes on the osmotic pressure of protein solutions is due to the isolated protein ions since these alone are capable of causing a Donnan equilibrium across a membrane impermeable to the protein ions but permeable to most crystalloidal ions. 3. The similar influence of electrolytes on the viscosity of protein solutions is due to the submicroscopic solid protein particles capable of occluding water since the amount of water occluded by (or the amount of swelling of) these particles is regulated by the Donnan equilibrium. 4. These ideas are supported by the fact that the more the submicroscopic solid particles contained in a protein solution or suspension are transformed into isolated ions (e.g., by keeping gelatin solution for 1 hour or more at 45°C.) the more the viscosity of the solution is diminished while the osmotic pressure is increased, and vice versa.


Sign in / Sign up

Export Citation Format

Share Document