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Keywords

HSA, organochlorine pesticides, fluorescence spectroscopy

Abstract

Human serum albumin (HSA) is the most abundant blood plasma protein and plays a crucial role in drug transport and physiological homeostasis. HSA has a highly flexible structure consisting of three domains, each with multiple binding sites lined with hydrophobic and hydrophilic residues. The structural properties of HSA make it a robust reservoir and receptor for various endogenous and exogenous compounds, including therapeutic drugs. Organochlorine pesticides (OCPs) are a subclass of pesticides characterized by their chlorine content. Once widely used, these compounds remain persistent in the environment and biological systems despite regulatory restrictions in many developed countries. The strong ligand-binding affinity of HSA, while advantageous in some instances, also allows for interactions with persistent small molecules like OCPs. These interactions can lead to structural and functional alterations in the protein, potentially impacting its physiological role. Changes in HSA structure caused by OCP binding may affect its ability to transport essential molecules, disrupt normal biological functions, and contribute to toxic effects in exposed organisms. In this review, we have reviewed the interaction of HSA with common organochlorine pesticides.

MS3563_HSA-Organochlorine review_Revised final.pdf (824 kB)
Revised after minor revision

MS3563_Response to reviewers comments_final.pdf (89 kB)
Response to reviewer

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