Diabetes is high blood glucose. Diabetes can be classified into Type 1 diabetes and Type 2 diabetes according to the cause and pathophysiology. The hormone insulin is released from the cells of your pancreas. Both these activities of insulin help it do so: by directing glucose into the human cells for storing or burning; by providing glucose to the cells to lower blood glucose. If diabetes patients cannot process the blood sugar because they don't have enough pancreatic insulin production (type 1 diabetes) or they have insulin resistance (type 2 diabetes), blood sugar will spike. Insulin is inextricably connected to patients with type 1 diabetes, because we require insulin to compensate for the body's lack of insulin. Usually, if the patient is under such an adverse effect for some time, the doctor would convert the patient's diet, exercise, and medications to the injection of insulin. Virus drugin (created by restructuring DNA) is a genetically engineered version and the biggest breakthrough in diabetes. Natural/correct insulin is found mostly in the pancreas of animals (pigs, cows) and reconstituted insulin is generated by transfecting human insulin genes into E coli or yeast.
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The Harm of Diabetes
Diabetes is a kind of metabolic chronic disease, mainly characterized by abnormal blood sugar levels. The hazards of diabetes are mainly reflected in cardiovascular disease, kidney damage, eye disease, nerve damage, feet complications, teeth and oral health, and the risk of infection. Infection risk increases. The harm of diabetes not only affects physical health, but also has a profound impact on mental health and quality of life. Therefore, the timely intervention and management of diabetes is essential.
Recombinant Insulin
Recombinant insulin, the kind of insulin that is genetically engineered to treat diabetes. Recombinant human insulin is a protein whose 51 amino acids are sequences from recombinant DNA. Recombinant insulin: Genes for human insulin are implanted in Escherichia coli or yeast such that the bacteria creates human insulin in the same shape and form. Host DNA and proteins left over from host cells in recombinant human insulin are production contaminants, and must not be used in production. Their boundaries must be legal. Recombinant insulin is the new drug. That fake insulin is made by the most sophisticated biotechnology.
| Structure |
Description |
| Amino Acids |
A chain (21 amino acids) and B chain (30 amino acids) |
| Molecular Weight |
5800 Da |
| Host Cells |
Escherichia coli |
| Contents |
1mg contains no less than 27.5 units of recombinant human insulin |
| Connections |
Covalently linked by disulfide bonds |
| Advantages |
High purity, good biocompatibility, strong production controllability |
Fig. 1 Structure of insulin (Kjeldsen, T., et al. 2024).
Since the successful expression of insulin in E. coli, researchers have been exploring the selection and improvement of the expression system of insulin genes. Not only has the biosynthesis of human insulin in microorganisms been achieved and brought to market, but it has also promoted and accelerated the research process of protein genetic engineering in other mammals.
Saccharomyces Cerevisiae and Recombinant Insulin
Saccharomyces cerevisiae: The fungus fermentation can employ, is the most common yeast used for beer, wine, and bread. Saccharomyces cerevisiae, another expression system used for recombinant proteins (recombinant insulin, for example) in biotech. Annual insulin drug demand is more than 40 tons, with the other half generated through recombinant secretory activity of Saccharomyces cerevisiae. Create recombinant insulin and also you have a way to treat the diabetes. Recombinant insulin is less allergenic than animal insulin.
Molecular Engineering to Optimize Recombinant Secretory Expression of Insulin
The molecular pharmacology of insulin is at the heart of insulin analogs and its pharmacokinetic and pharmacodynamic properties can be optimised by changing its properties. If you make insulin clinically more attractive by adding amino acids, that will change the properties of the corresponding single-chain precursor. So the biophysical structure of the related insulin precursor could have to be modulated for its successful synthesis in scerevisiae.
Current Status of Recombinant Insulin Development
Recombinant insulin has always been an innovation-and-improvement-heavy enterprise. Since recombinant insulin was approved for use in 1982, to the present day when many different insulin analogs are appropriate for different patients, the life cycle of this central hormone has been astonishing. In type 2 diabetes, where insulin resistance and relative insulin deficiency are common, recombinant insulin therapy can help to manage the disease and avoid complications of uncontrolled hyperglycemia. Recombinant insulin speaks to the wonders of biotechnology and pharmaceutical science. This synthetic hormone made a dramatic difference in the treatment of diabetes, and is still a hope for patients with the debilitating condition.
Conclusion
Recombinant production at industrial scale is essential for getting new peptide or protein therapeutics from bench to clinic. Recombinant insulin is still needing optimization. Whether the expression vector and promoter are chosen to be responsible for recombinant expression is of critical importance, as are overexpression (e.g., chaperones or protein disulfide isomerases) and the conditions of fermentation (e.g., media composition, growth parameters). Such things have been studied deeply in order to support and optimise expression.
References
- Bhoria, S., et al. Current advances and future prospects in production of recombinant insulin and other proteins to treat diabetes mellitus. Biotechnology Letters. 2022, 44(5): 643-669.
- Kjeldsen, T., et al. Molecular engineering of insulin for recombinant expression in yeast. Trends in Biotechnology. 2024, 42(4): 464-478.
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