Effects of human serun albumin in some biological properties of rhodium(II) complexes

Abstract

were determined by spectrophotometry. In the case of the alkylcarboxylates, an inverse correlation of affinity with their liposolubilities was observed. Diffusion of the free or protein-bound complexes into Ehrlich cells in vitro seems to be primarily governed by the hydrophobic character of the complex. The complex [Rh 2 (tfc) 4 ] exhibited affinity towards the protein (K = 214.1) as well as cell partition both in the absence (32.1%) and presence (48.6%) of HSA. The compound HSA: [Rh 2 (tfc) 4 ] has had its antitumoral action in tumor-bearing Balb-c mice investigated, showing that HSA can be a drug reservoir for the rhodium complex.

Unusual Structural Features in the Adduct of Dirhodium Tetraacetate with Lysozyme

“…Due to their possible role in the definition of the mechanism of action of these potential anticancer agents, the interactions of [Rh 2 (μ-O 2 CCH 3 ) 4 ] with amino acids, peptides, and proteins have been studied, but contrasting results have been reported in the literature [ 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 ]. Reaction of [Rh 2 (μ-O 2 CCH 3 ) 4 ] with Cys and its derivatives and with glutathione leads to oxidation of the Rh(II)–Rh(II) dimeric unit and formation of Rh(III)–Rh(III)-containing dimeric and oligomeric species [ 21 ].…”

Kinetic and mechanistic studies on the interaction ofDL -Penicillamine with the hydroxopentaaquarhodium(III) ion

“…Recently the interaction of rhodium(II) and other platinum group metal antitumoral compounds with serum albumin has been reported by Esposito and Najjar [1], where rhodium is thought to react mainly through coordination with the imidazole group of histidine residues. In some earlier studies a series of antitumoral rhodium(II) carboxylates, for example, Rh 2 (CH 3 CO 2 ) 4 , Rh 2 (CH 3 CH 2 CO 2 ) 4 , Rh 2 (CH 3 CH 2 CH 2 CO 2 ) 4 and Rh 2 (CF 3 CO 2 ) 4 were found to bind quickly to albumin [2]. The interactions of DL-methionine [3] and L -cysteine [4] with hydroxopentaaquarhodium(III) ion have been reported.…”

Exploring a Reaction Mechanism for Acetato Ligand Replacement in Paddlewheel Tetrakisacetatodirhodium (II,II) Complex by Ammonia: Computational Density Functional Theory Study

“…The affinity of paddle-wheel dirhodium complexes with Trp 214 in human albumin was explored in studies. 28,29 Recently, reactivity with a dirhodium complex with two bridging aspartate side chains in natural peptide sequences was also explored by Sambasivan et al 30 Recently, an interesting computational study on the dependence of chemical shift on various axial (in the Rh-Rh axis) or equatorial (in positions perpendicular to the Rh-Rh axis) imidazole ligands in dirhodium paddle-wheel complexes was published. 31 Another study investigated the strength of Rh-Rh binding interaction under the influence of various axial ligands.…”

“…The affinity of paddle-wheel dirhodium complexes with Trp 214 in human albumin was explored in studies. , Recently, reactivity with a dirhodium complex with two bridging aspartate side chains in natural peptide sequences was also explored by Sambasivan et al…”