The backbone structure of fast acting insulin looks identical to normal hexameric insulin.
This model identifies the hydrogen bonds and sulfur bonds within fastacting insulin.Notice the two disulfide bonds attach the alpha and beta chains, and one other disulfide bond attaches two parts of the alpha chain to itself
In this engineered fast-acting insulin, the proline is changed to aspartate, shown in magenta. This weakens the interactions between the beta chains and allows it to break apart easier and faster
The presence of threonine(red) in the fast-acting insuline is the same as in human insulin. In the slow-acting insuline, the threonine is missing.
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Slow-Release Insulin
(based on 4AJX.pdb)
A backbone model of the six monomers of insulin shown in separate colors. Together they make up the hexameric insulin.
Here the monomers are shown colored by the chain type; A(green) and B(blue) chain
A single dimer of slow-acting insulin (degludec) is shown. The alpha chains are shown in green and are identical to normal human insulin. The beta chains are slightly different than human insulin in that one amino acid is removed(Theorine30) and instead a hexadecanoic acid (not shown) is attached to lys29 shown in red. (only one of the beta chains has lys 29 shown)
In the slow acting insulin monomer degludec, proline, colored in purple, is in the same spot as human insulin, and can be compared to the fast acting insulin monomer aspart, where in the same position, aspartate is found, colored in magenta on the fast acting model.
Locations where the theorine was removed and long chain hydrocarbons added (acylation)which causes buildup of insulin hexamers. This buildup doesn't allow for insulin to be easily dissolved allowed to lower blood sugar.
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References:
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4486707/
https://dmsjournal.biomedcentral.com/articles/10.1186/s13098-015-0037-0