The correlation of structural and binding affinity of insulin analog to the onset of action for diabetic therapy

Abstract
Background: These days, insulin analog production has been improved and becoming popular. The
advantages of insulin analog have been extensively reviewed in terms of effectiveness compared to human
insulin. Each of the insulin analog industries has claimed their safety and efficacy based on in vivo and in
vitro to overcome type 2 diabetes. Hereby, we report on the identification of highly effective analog-based
insulin on structure and binding affinity computationally, to confirm its potential and give a broader point
of view to insulin analog users.
Methods: Five types of insulin analogs, Aspart, Glargine, Detemir, Lispro and Degludec, were analyzed.
We grouped and clustered the sequence by alignment to identify the closeness and sequence similarity
between samples, continued by superimposing analysis and undertaking binding affinity identification
utilizing of a docking analysis approach.
Results: Lispro had the least sequence similarity to other types, close to Aspart (96%) and Glargine (90.5%),
while Detemir and Degludec showed 100% similarity we decide to only use Degludec for the next analysis.
Furthermore, Lispro, Aspart, and Glargine exhibited structural similarity strengthened by the lack of significant
difference in the RMSD data. Importantly, Aspart had the highest binding affinity score (-66.1 +/- 7.1 Kcal/mol)
in the docking analysis to the insulin receptor (INSR) and similar binding site areas to human insulin.
Conclusion: Our finding revealed that the strength of insulin analogs towards insulin receptors is identic