ArticleRSC advances2023
Structural modulation of insulin by hydrophobic and hydrophilic molecules.
Article in RSC advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Human Insulin Enhances Avobenzone Photostability while Retaining Its Biological Activity.ACS omega · 2026Article
- Hydrophobicity Study of Melamine, 1,3,5-Benzenetricarbonitrile, and 1,3,5-Triaminobenzene.ACS omega · 2026Article
- High-Throughput Analysis of Protein Adsorption to a Large Library of Polymers Using Liquid Extraction Surface Analysis-Tandem Mass Spectrometry (LESA-MS/MS).Analytical chemistry · 2025Article
- Assessment ofMolecular pharmaceutics · 2025Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
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