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Vol 14, 2025
Pages: 289 - 294
Original scientific paper
Engineering, Technology and Materials Editor: Darjana Sredić
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Received: 21.08.2025. >> Accepted: 14.10.2025. >> Published: 21.11.2025. Original scientific paper Engineering, Technology and Materials Editor: Darjana Sredić

INTERACTIONS OF HUMAN SERUM ALBUMIN WITH A PALLADIUM(II) COMPLEX CONTAINING A THIOAMIDE MOIETY: DETAILED EXPERIMENTAL AND MOLECULAR DOCKING STUDIES

By
Marija Ristić ,
Marija Ristić
Contact Marija Ristić

Faculty of Science, University of Kragujevac , Kragujevac , Serbia

Maja Đukić ,
Maja Đukić

Faculty of Science, University of Kragujevac , Kragujevac , Serbia

Jelena Petronijević ,
Jelena Petronijević

Faculty of Science, University of Kragujevac , Kragujevac , Serbia

Ivan Jakovljević ,
Ivan Jakovljević

Faculty of Science, University of Kragujevac , Kragujevac , Serbia

Marina Ćendić Serafinović ,
Marina Ćendić Serafinović

Faculty of Science, University of Kragujevac , Kragujevac , Serbia

Nenad Joksimović ,
Nenad Joksimović

Faculty of Science, University of Kragujevac , Kragujevac , Serbia

Milena Vukić
Milena Vukić

Faculty of Science, University of Kragujevac , Kragujevac , Serbia

Abstract

Thioamides and their derivatives are an interesting group of compounds because of their structural variations and also because of the combination of hard and soft donor atoms (S and N) that potentially allow coordination – in a variety of binding modes – to a wide range of metal centers, and also because of their biological significance.

In our previous studies, we have synthesized a palladium(II) complex with a thioamide-type ligand of the formula [PdL2Cl2] (L= ethyl 4-[1-amino-2-cyano-3-(methylamino)-3-thioxo-1-propen-1-yl]-1-piperazine-1-carboxylate), whose ability to interact with DNA was investigated fluorometrically. In this work, research was continued in the direction of studying the interactions of the thioamide ligand and its palladium(II) complex with human serum albumin (HSA) in the presence of site-specific markers: warfarin (site I, subdomain IIA), ibuprofen (site II, subdomain IIIA) or methyl orange (site III, subdomain IB), to determine the binding affinity, binding strength and the location of binding site. The results obtained showed that ligand and complex bind moderately to the HSA via site III (subdomain IB), and that the quenching mechanism is static.

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