Computational toxicity profiling of the UV stabilizer UV-328 against the human brain enzyme acetylcholinesterase

One of the current environmental pollutants of concern is the widespread use of the ultraviolet stabilizer UV-328, which has the potential to cause neurotoxicity. This study aimed to investigate the potential neurotoxicity of UV-328 by examining the possible interaction of UV-328 with human acetylcholinesterase through an integrated in silico methodology. The canonical active site pocket (C2) was identified as the preferred binding site, and UV-328 had a binding affinity of -8.5 kcal/mol, similar to that of tacrine and rivastigmine, and significantly weaker compared to that of the co-crystallized ligand, E20, which had a binding affinity of -12.1 kcal/mol. The stability of the UV-328-AChE complex was also observed during the 100 ns molecular dynamics simulation, as shown by the stable root mean square deviation (In silico predictions of ADMET and CNS penetration also indicated that UV-328 has physicochemical characteristics that are consistent with blood-brain barrier permeation. Collectively, these results suggest that a relatively stable interaction between UV-328 and acetylcholinesterase is possible, which supports the hypothesis of potential neurotoxic relevance of the compound and warrants further investigation. Reuslts are hypothetical and require experimrntal validation.