The Industrial Chemistry Scientific Research Laboratory Director at Baku State University (BSU), Alakbar Huseynzade, along with Ulviyya Hasanova, Chair of Biomedical Materials at ICESCO, Aygün Israyilova from the Microbiology and Virology Scientific Research Laboratory, Goncha Eyvazova, Lead Researcher at the Nano Research Scientific Research Laboratory, and Sanam Huseynova, Head Teacher of the Department of Biotechnology, collaborated on an article titled "Synthesis, nanostructuring, and in silico studies of a novel imine bond-containing macroheterocycle as a promising PBP-2a non-β-lactam inhibitor," which was published in the "Journal of Materials Chemistry B" (Impact Factor: 7.0, Q1 category).

https://pubs.rsc.org/en/content/articlelanding/2023/tb/d3tb00602f/unauth

The research focuses on synthesizing a forty-membered macro heterocycle through [2+2] cyclocondensation with diamine and aromatic dialdehyde, followed by nanostructuring it with magnetic nanoparticles. The structure of the macroheterocycle was analyzed using 1H and 13C Nuclear Magnetic Resonance spectroscopy and MALDI mass spectrometry. Subsequently, a nano supramolecular complex of the macro heterocycle with magnetite nanoparticles was created and characterized using IR and UV spectroscopy methods, with a loading efficiency of 18.6%. Transmission Electron Microscopy revealed nanospherical particles with diameters ranging from 10 to 20 nm.

The antibacterial activity of both the macro heterocycle and its nano supramolecular complex was tested against Klebsiella pneumoniae, Pseudomonas aeruginosa, and Staphylococcus aureus. The results demonstrated that the complex exhibited significantly higher activity against Staphylococcus aureus compared to the individual macroheterocycle, being 64 times more effective, and 32 times better than the antibiotic Ampicillin.

Furthermore, an in silico analysis of the macroheterocycle was conducted at the B3LYP/6-31G level, revealing its interaction with the Penicillin-binding protein PBP2a (5M18) from the transpeptidase family in Staphylococcus aureus during molecular docking studies.