Size- and surface functionalization-driven molecular interaction of CdSe quantum dots with jack bean urease:...

Quantum dots (QDs) with distinctive optical properties have been extensively researched and developed for usage in solar cells, imaging, drug delivery, cellular targeting, etc. But the inevitable production of QDs can lead to their unavoidable release and increased environmental concentration. Depending on morphological and surface properties, QDs at the nano-bio interface considerably impact the activity and structure of bio-molecules. The present study investigates the interaction of metalloenzyme jack bean urease (JBU) and bi-sized CdSe QDs (2.43 nm and 3.63 nm), surface-functionalized to mercaptopropionic acid (MPA) (-COOH), L-cysteine (CYS), L-glutathione (GSH), N-acetyl L-cysteine (NAC) (-COOH, -NH₂), and cysteamine hydrochloride (CYST) (-NH₂) to assess any alterations in JBU's binding, microenvironment, structure, exciton lifetime, and activity. JBU catalyzes the hydrolysis of urea to produce ammonia and carbon dioxide; any changes in its properties could threaten the survival of several microbes and plants. Spectroscopy techniques such as UV-Vis, fluorescence, circular dichroism, synchronous, time-resolved fluorescence, atomic force microscopy, and JBU activity assay were studied. Results suggested highly spontaneous and energy-favored interactions, which involved static quenching and hydrophobic forces of varied magnitude, dependent on QDs properties. The size, surface modifications, and dosage of QDs significantly impacted the secondary structure and activity of JBUs. Even though the larger sizes of the relevant modifications demonstrated stronger binding, the smaller sizes had the greatest impact on α-helicity and activity. CYST-capped QDs with an average number of the binding site (n) = 1, reduced α-helicity by 16% and activity by 22-30% at 7 nM concentration. In contrast, MPA-capped QDs with n < 1 had the least effect on α-helical structure and activity. The smaller GSH-capped QDs increased the activity by 9%, via partially restoring JBU's α-helical content. The study thus thoroughly analyzed the impact of varied-size and surface-functionalized QDs on the structure and function of JBU, which can be exploited further for several biomedical applications.