Published January 9, 2024 | Version v1
Journal article Open

Spectroscopic and thermodynamic characterization of the interaction of a new synthesized antitumor drug candidate 2H4MBBH with human serum albumin

Authors/Creators

  • 1. Medical University of Sofia, Sofia, Bulgaria
  • 2. Sofia University "St. Kliment Ohridski", Sofia, Bulgaria
  • 3. Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, Sofia, Bulgaria

Description

In the present work we studied the interactions of a newly synthesized drug candidate, 2-(2-hydroxy-4-methoxybenzylidene)-1-(1H-benzimidazol-2-yl)hydrazine (2H4MBBH), with human serum albumin (HSA) by fluorescence spectroscopy.

2H4MBBH-HSA binding parameters were assessed by fluorescence quenching strategy. As made clear by the concentration data, 2H4MBBH unequivocally quenched the instrinsic HSA fluorescence. The calculated Stern-Volmer quenching constant Ksv, the Ka of 2H4MBBH-HSA complexes, as well as the thermodynamic parameters ∆H°, ∆S° and ∆G°, showed that the H-bonding forces play major part in the interaction of 2H4MBBH with HSA. These calculations point to a quenching component based on 2H4MBBH-HSA static complex formation rather than energetic collisions.

Files

PHAR_article_112385.pdf

Files (805.8 kB)

Name Size Download all
md5:00e5658430605a438d807834e46145ba
761.6 kB Preview Download
md5:308ba6ab2403be13304e3307b499a0ae
44.2 kB Preview Download

Additional details

Cites
Publication: 10.1016/j.cbi.2021.109540 (DOI)
Publication: 10.1039/D1RA07419A (DOI)
Publication: 10.3390/molecules28010291 (DOI)
Publication: 10.15171/apb.2016.063 (DOI)
Publication: 10.1021/ic101534n (DOI)
Publication: 10.1021/bi00745a020 (DOI)
Publication: 10.1007/978-1-4615-7658-7 (DOI)
Publication: 10.1007/978-0-387-46312-4 (DOI)
Publication: 10.1016/j.jinorgbio.2020.111305 (DOI)
Publication: 10.1016/j.jphotochemrev.2012.09.001 (DOI)
Publication: 10.1021/bi00514a017 (DOI)
Has part
Figure: 10.3897/pharmacia.71.e112385.figure1 (DOI)
Figure: 10.3897/pharmacia.71.e112385.figure3 (DOI)
Figure: 10.3897/pharmacia.71.e112385.figure2 (DOI)
Figure: 10.3897/pharmacia.71.e112385.figure4 (DOI)

References

  • Kameliya A, Argirova M, Tzoneva R, Uzunova V, Mavrova A, Vuchev D, Popova-Daskalova G, Fratev F, Guncheva M, Yancheva D (2021) 1H-benzi midazole-2-yl hydrazones as tubulin-targeting agents: Synthesis, structural characterization, anthelmintic activity and antiproliferative activity against MCF-7 breast carcinoma cells and molecular docking studies. Chemico-Biological Interactions 345: 109540. https://doi.org/10.1016/j.cbi.2021.109540
  • Argirova M, Georgieva MK, Hristova-Avakumova NG, Vuchev DI, Popova-Daskalova GV, Anichina KK, Yancheva DY (2021) New 1H-benzimidazole-2-yl hydrazones with combined antiparasitic and antioxidant activity. RSC Advances 11: 39848–39868. https://doi.org/10.1039/D1RA07419A
  • Argirova M, Guncheva M, Momekov G, Cherneva E, Mihaylova R, Rangelov M, Todorova N, Denev P, Anichina K, Mavrova A, Yancheva D (2023) Modulation Effect on Tubulin Polymerization, Cytotoxicity and Antioxidant Activity of 1H-Benzimidazole-2-Yl Hydrazones. Molecules 28(1): 291. https://doi.org/10.3390/molecules28010291
  • Raoufinia R, Mota A, Keyhanvar N, Safari F, Shamekhi S, Abdolalizadeh J (2016) Overview of albumin and its purification methods. Advanced Pharmaceutical Bulletin 6(4): 495–507. https://doi.org/10.15171/apb.2016.063
  • Bhat SS, Kumbhar AA, Heptullah H, Khan AA, Gobre VV, Gejji SP, Puranik VG (2010) Synthesis, electronic structure, DNA and protein binding, DNA cleavage, and anticancer activity of fluorophore-labeled copper (II) complexes. Inorganic Chemistry 50: 545–558. https://doi.org/10.1021/ic101534n
  • Lakowicz JR, Weber G (1973) Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry 12(21): 4161–4170. https://doi.org/10.1021/bi00745a020
  • Lakowicz JR (1983) Principles of Fluorescence Spectroscopy. Plenum Press: New York and London, Chapter 9, 496 pp. https://doi.org/10.1007/978-1-4615-7658-7
  • Lakowicz JR (2006) Principles of Fluorescence Spectroscopy (3rd edn.). Springer, New York, 954 pp. https://doi.org/10.1007/978-0-387-46312-4
  • Macii F, Biver T (2020) Spectrofluorimetric analysis of the binding of a target molecule to serum albumin: tricky aspects and tips Journal of Inorganic Biochemistry 216: e111305. https://doi.org/10.1016/j.jinorgbio.2020.111305
  • Santhamani N, Sambandam A (2013) Binding of serum albumins with bioactive substances – Nanoparticles to drugs. Journal of Photochemistry and Photobiology C: Photochemistry Reviews 14: 53–71. https://doi.org/10.1016/j.jphotochemrev.2012.09.001
  • Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry 20(11): 3096–3102. https://doi.org/10.1021/bi00514a017