Analytical and Computational Insights Into Serum Albumin Interactions with Antiparkinsonian Drugs: A Comprehensive Review

Abstract Serum albumins play a critical role in drug pharmacokinetics by regulating the transport, distribution, and metabolism of pharmaceutical compounds. Understanding drug‐serum albumin interactions is essential for optimizing drug efficacy and minimizing adverse effects. This review systematically explores the binding properties of antiparkinsonian drugs with various serum albumins through experimental and computational approaches. Analytical techniques, including spectroscopic and electrochemical methods, have been widely used to investigate these interactions. Additionally, computational tools such as molecular docking and molecular dynamics (MD) simulations provide valuable insights into binding site preferences and interaction energies. The review offers a theoretical framework for antiparkinsonian drug‐protein interactions, focusing on key factors such as binding affinities, structural changes in serum albumin, alterations in the protein microenvironment, and specific binding sites. Furthermore, it discusses how these interactions affect drug pharmacokinetics and their potential impact on drug design and development. Unlike previous studies that either addressed general drug‐protein interactions or emphasized individual analytical techniques, this review presents a comprehensive analysis of antiparkinsonian drug‐serum albumin binding by integrating multiple methodologies. This integrated understanding may contribute to the development of more effective drug formulations and support personalized treatment strategies for Parkinson's disease.