Pregled bibliografske jedinice broj: 1171196
Synthesis, characterization and investigating the binding mechanism of novel coumarin derivatives with human serum albumin: Spectroscopic and computational approach
Synthesis, characterization and investigating the binding mechanism of novel coumarin derivatives with human serum albumin: Spectroscopic and computational approach // Journal of molecular structure, 1254 (2022), 132366, 14 doi:10.1016/j.molstruc.2022.132366 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 1171196 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Synthesis, characterization and investigating the
binding mechanism of novel coumarin derivatives
with human serum albumin: Spectroscopic and
computational approach
Autori
Avdović, Edina ; Milanović, Žiko ; Molčanov, Krešimir ; Roca, Sunčica ; Vikić-Topić, Dražen ; Mrkalić, Emina ; Jelić, Ratomir ; Marković, Zoran
Izvornik
Journal of molecular structure (0022-2860) 1254
(2022);
132366, 14
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
4-hydroxycoumarin ; HSA ; Molecular docking ; Molecular dynamic
Sažetak
Two 4-hydroxycoumarin derivatives: (E)-3-(1- ((4‑hydroxy-3-methoxyphenyl)amino) - ethylidene)chromane-2, 4‑dione (L1) and (E)-3-(1- ((3‑hydroxy-4-methoxyphenyl)-amino)ethylidene) chromane-2, 4‑dione (L2), were prepared and structurally characterized by spectroscopic techniques in combination with the B3LYP-D3BJ theoretical method. The interactions between newly synthesized compounds and human serum albumin (HSA) were investigated under physiological conditions at 296, 303, and 310 K by fluorescence and absorption spectroscopy, molecular docking, and molecular dynamic simulations. The results of absorption and fluorescence spectral analysis showed that ligands quenched HSA fluorescence through a static process. The corresponding thermodynamic parameters ΔH0, ΔS0, and ΔG0 were calculated according to Van't Hoff's equation. The obtained results indicated that compounds bind spontaneously to HSA mainly by van der Waals's forces and through hydrogen bonds. Ligand- competitive displacement experiments, using known site-specific ligands for HSA's binding sites (I and II) suggest that ligands had a higher affinity for site I (subdomain IIA). The results of the computational analysis follow the experimental data, and the obtained results suggest that the investigated compounds show a good binding affinity according to the HSA receptor, which will be useful for future studies related to rational drug design.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Ustanove:
Institut "Ruđer Bošković", Zagreb,
Sveučilište Jurja Dobrile u Puli
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
