Abstract
Antibody based drugs are increasingly being used to treat a vast array of diseases because of their unique affinity to target specific antigen proteins on the surfaces of target cancer cells. Fusions of antibodies and conjugated biopharmaceuticals are progressively being used as this gives the opportunity to target other cytotoxic molecules to unwanted cells. It is critical to ensure these types of drug products are not fragile or uneconomical to produce at a large scale. A very small amount of precious protein solution can be characterised in an Ultra scale-down (USD) shear device to uncover if fusion proteins are prone to shear stress. This article presents how the purified and deglycosylated form of the MFECP1 fusion protein was quantified with an ELISA from 700-50 ng/ml, with a +/- 10% deviation in the standard curve. It also describes how the same MFECP1 fusion protein was analysed to establish the optimum experimental control conditions that were required to observe changes due to hydrodynamic-associated degradation in a shear device. Lastly, it looks at how a first order kinetic relationship can be used to model the rate of MFECP1 fusion protein degradation and how this was used to quantify the rate of protein loss during different shear environments with and without air/liquid interfaces.
Highlights
The advancement of modern medicine has propagated an ageing population; disorders like cancer, dementia and neurodegradative diseases are becoming more common and are difficult to treat with traditional synthetic chemical compounds
In conclusion it has been shown that a Ultra scale-down (USD) shear device can be used to characterise antibody fusion proteins in controlled conditions
It has been described that the fusion protein under investigation contained a glycosylated variant and deglycosylation experiments showed that a more refined fusion protein product could be used in shear experiments, reducing variability in experiments
Summary
The advancement of modern medicine has propagated an ageing population; disorders like cancer, dementia and neurodegradative diseases are becoming more common and are difficult to treat with traditional synthetic chemical compounds These diseases require the manufacture of very complicated biopharmaceuticals; fusion proteins and conjugated drugs [1, 2, 16, 22]. Better understanding of how these complexes breakdown and how they can be minimised, would help a process engineer to improve the large scale bioprocessing of biopharmaceuticals An example of this type of research can be found in the work cover by [5, 11] where it was found that ultra scale-down techniques have uncovered shear protectants that could be added to the large scale process to improve yield impurities
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