Insulin is a protein derived from the pancreas that regulates the metabolism of sugar in the body. How is it structured? How does it work?
The structure of insulin, like other proteins, is a peptide chain consisting of several amino acids. It has 51 amino acids arranged into 2 chains A and B according to a certain pattern. And they are linked together side by side by 3 disulfide bonds. Under normal circumstances 6 such insulins are interlinked and polymerized together to keep them in a stable state. This is especially true for synthetic or purified insulin. Junming Hu, Department of Endocrinology and Nephrology, Baicheng Hospital
The structure of insulin also determines its onset of action. We all know that it takes 30 minutes for subcutaneous injection of short-acting insulin to be ready for meals. In other words, short-acting insulin starts to work only 30 minutes after injection. Why? Because insulin only works as a monomer, and it takes about 30 minutes to break down from a 6-member into a monomer.
Because of this property of insulin, people add other proteins to prolong the action time of insulin for different therapeutic purposes. For example, adding fisetin at a ratio of 1:1 forms medium-acting insulin, and adding fisetin at a ratio of 1:2 forms long-acting insulin. It can be applied for different purposes.
Before people could not synthesize insulin, insulin was usually extracted from the pancreas of animals. However, such insulin is different from the real human insulin, and the closest animal insulin to human insulin is pig and cow. It differs from human insulin by one and two amino acids, respectively. Although it is different from human insulin, it can be used in human after purification and has a hypoglycemic effect. The use of animal insulin for the treatment of diabetes has been around for a hundred years and it has promoted the treatment of diabetes.
With the deepening of the research on diabetes and insulin and the innovation of science, people can use the method of genetic recombination to produce human insulin in large quantities by biological methods according to the order of amino acid arrangement of human insulin to meet the needs of diabetes treatment. However, people are not satisfied with this status quo, and in response to the shortage of insulin’s long onset time and long peak time, the amino acids in a certain part of insulin peptide chain are exchanged, replaced or linked with other amino acids to arrive at a new structure of protein, which exists in a monomeric state, is easily absorbed, has no peak effect smoothly, and is synchronized with the peak of blood glucose, especially postprandial blood glucose, and also has the effect of lowering blood glucose. This protein is called an insulin analogue. The main insulin analogues are: lysergic acid insulin; menthol insulin; and glargine insulin, which have been widely used in the treatment of diabetic patients and have achieved good therapeutic effects.
We believe that the progress of insulin research will bring a more reliable, convenient and effective treatment route for diabetes. It brings confidence and hope to overcome diabetes.