Akademik Veri Yönetim Sistemi
Luminescence, cilt.40, sa.8, 2025 (SCI-Expanded)
Dehydroepiandrosterone (DHEA), a naturally occurring steroidal hormone precursor, has attracted considerable scientific interest due to its diverse pharmacological activities, including anti-inflammatory, antioxidant, and protease-modulatory effects. In this study, we systematically investigated the binding interactions of DHEA with three biologically relevant targets: trypsin, calf thymus DNA (CT-DNA), and human serum albumin (HSA). The effects of DHEA on the structure and activity of these macromolecules were carried out using fluorescence spectroscopy, FTIR, and molecular docking techniques. Molecular docking simulations revealed that DHEA forms stable complexes with all three macromolecules, exhibiting the highest affinity toward HSA (−8.71 kcal mol−1), followed by trypsin (−6.30 kcal mol−1) and DNA (−6.15 kcal mol−1). DHEA was found to bind within the minor groove of DNA through hydrogen bonds and van der Waals interactions, occupy Subdomain IB of HSA stabilized by hydrophobic contacts, and interact near the catalytic triad of trypsin through alkyl and π–alkyl interactions. In silico ADMET profiling predicted favorable drug-like properties, including high gastrointestinal absorption, blood–brain barrier permeability, and low toxicity risk. These findings highlight the multitarget potential of DHEA and support its relevance as a pharmacologically versatile molecule capable of modulating nucleic acids, transport proteins, and proteolytic enzymes.