Structural modulation of insulin by hydrophobic and hydrophilic molecules

In the bloodstream, insulin interacts with various kinds of molecules, which can alter its structure and modulate its function. In this work, we have synthesized two molecules having extremely hydrophilic and hydrophobic side chains. The effects of hydrophilic and hydrophobic molecules on the binding with insulin have been investigated through a multi-spectroscopic approach. We found that hydrophilic molecules have a slightly higher binding affinity towards insulin. Insulin can bind with the hydrophilic molecules as it binds glucose. The high insulin binding affinity of a hydrophobic molecule indicates its dual nature. The hydrophobic molecule binds at the hydrophobic pocket of the insulin surface, where hydrophilic molecules interact at the polar surface of the insulin. Such binding with the hydrophobic molecule perturbs strongly the secondary structure of the insulin much more in comparison to hydrophilic molecules. Therefore, the stability of insulin decreases in the presence of hydrophobic molecules. In the bloodstream, insulin interacts with various kinds of molecules, which can alter its structure and modulate its function.

Automated summary

Insulin interacts with molecules in the bloodstream, with hydrophilic and hydrophobic molecules having different effects on its binding and structure. Hydrophilic molecules have a slightly higher binding affinity towards insulin, while hydrophobic molecules bind to a specific pocket on the insulin surface and strongly perturb its secondary structure.