Exploring the Biomaterial Potential of a Naphthalene-based Schiff Base through Protein Binding, Molecular Docking, MD Simulation, and Swiss-ADME analysis

Phenolic-based Schiff bases are highly interesting in biological applications due to their enhanced stability,
strong metal-chelating ability, and capacity to form hydrogen bonds and electrostatic interactions with biomolecules, which enhance their notable pharmacological and bioactive effects. A Schiff base ligand, (E)-1-(((2-
aminophenyl)imino)methyl)naphthalen-2-ol (OPN) was derived from 2‑hydroxy-1-naphthaldehyde and o-phenylenediamine. OPN was thoroughly characterized using standard spectroscopic and microscopic techniques,
such as FT-IR, NMR and HR-MS analysis. OPN was further investigated using density functional theory (DFT)
calculations to determine the HOMO–LUMO energy levels, and the derived global reactivity parameters provided
valuable insights into its chemical reactivity, kinetic stability, and electronic properties. Fluorescence quenching
analysis was used to check the binding interaction between bovine serum albumin (BSA) and OPN. The strong
binding interaction was confirmed by the obtained quenching rate constant (2.79 × 1013 M− 1 s− 1
) and a
moderate binding constant (7.14 × 105 M− 1
). Further, we performed the fluorescence quenching analysis at
different temperatures and confirmed that the quenching is due to static quenching. The experimental results
related to molecular docking analysis indicate that OPN binds strongly within the active sites of BSA. Moreover,
molecular dynamics simulations revealed that the BSA-OPN complex remained structurally stable for up to 50 ns,
indicating a stable, energetically favourable binding interaction. Swiss-ADME analysis was performed to assess
the pharmacokinetic and drug-likeness characteristics of OPN. Overall, this work highlights the significant
binding ability of the synthesized OPN with protein, suggesting its potential applicability towards biological
applications.