Spectroscopic and Theoretical Analysis of the Interaction between Plasma Proteins and Phthalimide Analogs with Potential Medical Application

Abstract

One of the groups of organic compounds with potential use in medicine and pharmacy is phthalimide derivatives. They are characterized by a wide range of properties such as antibacterial, antifungal, and anti-inflammatory. In this study, we focused on research on four phthalimide derivatives with proven non-toxicity, which are cyclooxygenase inhibitors. With the use of molecular docking study and spectroscopic methods, such as fluorescence, circular dichroism, and FT-IR spectroscopies, we analyzed the way the tested compounds interact with plasma proteins. Among the many proteins present in the plasma, we selected three: albumin, α1-acid glycoprotein, and gamma globulin, which play significant roles in the human body. The obtained results showed that all tested compounds bind to the analyzed proteins. They interact most strongly with albumin, which is a transport protein. However, interactions with serum albumin and orosomucoid do not cause significant changes in their structures. Only in the case of gamma globulins significant changes were observed in protein secondary structure.

Revealing the mechanistic interactions of profenofos and captan pesticides with serum protein via biophysical and computational investigations

“…However, its quenching rate constants ( ) was at a level of 10 12 M −1 s −1 , which was 100 times larger than the maximum diffusion rate (2 × 10 10 M −1 s −1 ) of the dynamic quenching process. This contradicted observation may suggest that complex formation plays a more significant role in the interaction between BSA and CT, rather than a dynamic process being the only driving factor, which was concurrent with a static mechanism of phthalimide analogs forming a stable complex with BSA 35 . However, further investigation is necessary to confirm this hypothesis.…”