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Human Insulin vs Genetically Engineered Fast Acting Insulins
Author(s) -
Mukhtar Farzan,
Veljkovic Petar,
Melnyk Max,
Smetanin Yakov,
Gong David,
Lawal Dayo,
Drohomyrecky Michael,
Mingolelli Gabrielle
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.lb213
Subject(s) - insulin , medicine , endocrinology , diabetes mellitus , insulin receptor , insulin oscillation , pancreas , glucose transporter , insulin resistance
Insulin is a protein produced in the pancreas. The primary function of insulin is to regulate the levels of glucose in the body from food that is consumed. When food is consumed, beta cells in the pancreas, the body is signalled to release insulin. The insulin that is released binds to insulin receptors, which then cause glucose transporters to be inserted in the membranes of different cells. The glucose transporters allow the cells to take in glucose from the bloodstream, and be used for energy for the body, or be stored for later use as glycogen. Individuals with diabetes are not able to produce sufficient insulin in the pancreas to keep blood glucose levels low, leading to health problems. One treatment for diabetes is to use insulin medication to control blood glucose levels. Due to the need for insulin medication which quickly takes action and lowers the blood glucose levels of diabetes patients, fast‐acting insulin was developed as a medication option. The structural differences between fast‐acting insulin medication, and insulin that is produced naturally in the pancreas are what cause the two proteins to function differently. Insulin lispro, which was the first genetically engineered rapid acting insulin, has a slight difference in the B chain than human insulin, where the proline at position 28 is switched with lysine at position 29, resulting in a lower capacity of self association in a solution, which results in a faster absorption, higher peak serum levels, and a shorter action duration than human insulin. Insulin aspart, another form of fast acting insulin, is structurally different from human insulin, in that the proline at position 29 is switched with a charged aspartic acid resulting in it being absorbed twice as fast as human insulin. Insulin glulisine, the most recently created fast acting insulin, is different in structure from human insulin because the asparagine at position 3 is replaced with lysine, and the lysine at position 29 is replaced with glutamic acid, which results in a reduction in hexamer formation and an enhanced absorption from subcutaneous depots. These differences in structure between the three different types of fast acting insulins and human insulin will be directly pointed out with the models of the different insulin types which will be created. Support or Funding Information Funded generously by Chicago Public Schools, the Cless Family Foundation, Friends of LIncoln Park High School, and the Center of Biomolecular Modeling at Milwaukee School of Engineering. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .