Binding mechanisms of half-sandwich Rh(III) and Ru(II) arene complexes on human serum albumin: a comparative study

Orsolya Dömötör, E. Enyedy

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Abstract: Various half-sandwich ruthenium(II) arene complexes and rhodium(III) arene complexes have been intensively investigated due to their prominent anticancer activity. The interaction of the organometallic complexes of Ru(η6-p-cymene) and Rh(η5-C5Me5) with human serum albumin (HSA) was studied in detail by a combination of various methods such as ultrafiltration, capillary electrophoresis, 1H NMR spectroscopy, fluorometry and UV–visible spectrophotometry in the presence of 100 mM chloride ions. Binding characteristics of the organometallic ions and their complexes with deferiprone, 2-picolinic acid, maltol, 6-methyl-2-picolinic acid and 2-quinaldic acid were evaluated. Kinetic aspects and reversibility of the albumin binding are also discussed. The effect of low-molecular-mass blood components on the protein binding was studied in addition to the interaction of organorhodium complexes with cell culture medium components. The organometallic ions were found to bind to HSA to a high extent via a coordination bond. Release of the bound metal ions was kinetically hindered and could not be induced by the denaturation of the protein. Binding of the Ru(η6-p-cymene) triaqua cation was much slower (ca. 24 h) compared to the rhodium congener (few min), while their complexes interacted with the protein relatively fast (1–2 h). The studied complexes were bound to HSA coordinatively. The highly stable and kinetically inert 2-picolinate Ru(η6-p-cymene) complex bound in an associative manner preserving its original entity, while lower stability complexes decomposed partly or completely upon binding to HSA. Fast, non-specific and high-affinity binding of the complexes on HSA highlights their coordinative interaction with various types of proteins possibly decreasing effective drug concentration. Graphic abstract: [Figure not available: see fulltext.].

Original languageEnglish
Pages (from-to)703-719
Number of pages17
JournalJournal of Biological Inorganic Chemistry
Volume24
Issue number5
DOIs
Publication statusPublished - Aug 1 2019

Fingerprint

Serum Albumin
Organometallics
Ions
Rhodium
Protein Denaturation
Capillary electrophoresis
Fluorometry
Proteins
Denaturation
Ruthenium
Spectrophotometry
Ultrafiltration
Capillary Electrophoresis
Molecular mass
Cell culture
Protein Binding
Nuclear magnetic resonance spectroscopy
Metal ions
Culture Media
Cations

Keywords

  • Albumin
  • Binding affinity
  • Capillary electrophoresis
  • Fluorescence
  • Ultrafiltration

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Binding mechanisms of half-sandwich Rh(III) and Ru(II) arene complexes on human serum albumin : a comparative study. / Dömötör, Orsolya; Enyedy, E.

In: Journal of Biological Inorganic Chemistry, Vol. 24, No. 5, 01.08.2019, p. 703-719.

Research output: Contribution to journalArticle

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