Τίτλος:
In vitro and in silico evaluation of the inhibitory effect of a curcumin-based oxovanadium (IV) complex on alkaline phosphatase activity and bacterial biofilm formation
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
Abstract: The scientific interest in the development of novel metal-based compounds as inhibitors of bacterial biofilm-related infections and alkaline phosphatase (ALP) deregulating effects is continuous and rising. In the current study, a novel crystallographically defined heteroleptic V(IV)-curcumin-bipyridine (V-Cur) complex with proven bio-activity was studied as a potential inhibitor of ALP activity and bacterial biofilm. The inhibitory effect of V-Cur was evaluated on bovine ALP, with two different substrates: para-nitrophenyl phosphate (pNPP) and adenosine triphosphate (ATP). The obtained results suggested that V-Cur inhibited the ALP activity in a dose-dependent manner (IC50 = 26.91 ± 1.61 μM for ATP, IC50 = 2.42 ± 0.12 μM for pNPP) exhibiting a mixed/competitive type of inhibition with both substrates tested. The evaluation of the potential V-Cur inhibitory effect on bacterial biofilm formation was performed on Gram (+) bacteria Staphylococcus aureus (S. aureus) and Gram (−) Escherichia coli (E. coli) cultures, and it positively correlated with inhibition of bacterial ALP activity. In silico study proved the binding of V-Cur at eukaryotic and bacterial ALP, and its interaction with crucial amino acids of the active sites, verifying complex’s inhibitory potential. The findings suggested a specific anti-biofilm activity of V-Cur, offering a further dimension in the importance of metal complexes, with naturally derived products as biological ligands, as therapeutic agents against bacterial infections and ALP-associated diseases. Key points: • V-Cur inhibits bovine and bacterial alkaline phosphatases and bacterial biofilm formation. • Alkaline phosphatase activity correlates with biofilm formation. • In silico studies prove binding of the complex on alkaline phosphatase. © 2020, Springer-Verlag GmbH Germany, part of Springer Nature.
Συγγραφείς:
Katsipis, G.
Tsalouxidou, V.
Halevas, E.
Geromichalou, E.
Geromichalos, G.
Pantazaki, A.A.
Περιοδικό:
Applied Microbiology and Biotechnology
Εκδότης:
Springer Science and Business Media Deutschland GmbH
Λέξεις-κλειδιά:
Adenosinetriphosphate; Binding sites; Biofilms; Escherichia coli; Mammals; Metal complexes; Vanadium compounds, ALkaline phosphatase; Alkaline phosphatase activity; Bacterial alkaline phosphatase; Dose-dependent manner; Escherichia coli (E. coli); Nitrophenyl phosphates; Oxovanadium complexes; Potential inhibitors, Phosphatases, adenosine triphosphate; alkaline phosphatase; antibiotic agent; curcumin; curcumin bipyridine complex; unclassified drug; alkaline phosphatase; curcumin, antibiofilm activity; Article; bacterial cell; bacterial growth; biofilm; crystallography; dose response; drug potency; drug screening; drug synthesis; enzyme activity; Escherichia coli; IC50; in vitro study; molecular docking; nonhuman; Staphylococcus aureus; animal; biofilm; bovine; computer simulation; Staphylococcus aureus, Bacteria (microorganisms); Bovinae; Escherichia coli; Eukaryota; Staphylococcus aureus, Alkaline Phosphatase; Animals; Biofilms; Cattle; Computer Simulation; Curcumin; Escherichia coli; Staphylococcus aureus
DOI:
10.1007/s00253-020-11004-0
