Application of capillary electrophoresis–inductively coupled plasma mass spectrometry to comparative studying of the reactivity of antitumor ruthenium(III) complexes differing in the nature of counter-ion toward human serum proteins

Pawlak, Katarzyna; Abramski, Jan K.; Ferenc, Julia; Foteeva, Lidia S.; Timerbaev, Andrei R.; Keppler, Bernhard K.; Jarosz, Maciej

doi:10.1016/j.chroma.2008.04.009

Cited by 45 publications

(30 citation statements)

References 12 publications

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“…Depletion with organic solvents revealed lower molecular mass proteins (Kay et al, 2008). ICP MS might be used to detect proteins that carry elemental labels (Polec-Pawlak et al, 2008;Razumienko et al, 2008). There are many possible novel combinations of technologies (Horvatovich et al, 2007;Baum et al, 2008;Dayarathna, Hancock, & Hincapie, 2008;Han & Speicher, 2008;Sihlbom et al, 2008;Tanaka et al, 2009).…”

Section: H Other Methodsmentioning

confidence: 98%

“…Blood proteins have been fractionated by free flow electrophoresis or capillary electrophoresis Hoffmann et al, 2001;Ebert et al, 2006;Johannesson et al, 2007;Polec-Pawlak et al, 2008;Wildgruber et al, 2008). Blood proteins and peptides have been identified and their patterns recorded, using capillary electrophoresis (Johannesson et al, 2007;Hernandez et al, 2008).…”

Section: G Iso-electric Focusing (Ief) Liquid and Capillary Electrmentioning

confidence: 99%

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Mass spectrometry of peptides and proteins from human blood

Zhu

Bowden

Zhang

et al. 2010

Mass Spectrometry Reviews

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It is difficult to convey the accelerating rate and growing importance of mass spectrometry applications to human blood proteins and peptides. Mass spectrometry can rapidly detect and identify the ionizable peptides from the proteins in a simple mixture and reveal many of their post-translational modifications. However, blood is a complex mixture that may contain many proteins first expressed in cells and tissues. The complete analysis of blood proteins is a daunting task that will rely on a wide range of disciplines from physics, chemistry, biochemistry, genetics, electromagnetic instrumentation, mathematics and computation. Therefore the comprehensive discovery and analysis of blood proteins will rank among the great technical challenges and require the cumulative sum of many of mankind's scientific achievements together. A variety of methods have been used to fractionate, analyze and identify proteins from blood, each yielding a small piece of the whole and throwing the great size of the task into sharp relief. The approaches attempted to date clearly indicate that enumerating the proteins and peptides of blood can be accomplished. There is no doubt that the mass spectrometry of blood will be crucial to the discovery and analysis of proteins, enzyme activities, and post-translational processes that underlay the mechanisms of disease. At present both discovery and quantification of proteins from blood are commonly reaching sensitivities of ∼1 ng/mL.

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Section: H Other Methodsmentioning

confidence: 98%

Section: G Iso-electric Focusing (Ief) Liquid and Capillary Electrmentioning

confidence: 99%

Mass spectrometry of peptides and proteins from human blood

Zhu

Bowden

Zhang

et al. 2010

Mass Spectrometry Reviews

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“…The influence of reducing agents on the binding behaviour of Ru(III) complexes KP1019 and KP418 towards the DNA model nucleotide was studied by CE coupled to ESI-MS [21]. The investigation of the reactivity of antitumor Ru(III) complexes towards human serum proteins was performed by the use of CE-ICP-MS [22,23]. A method based on combining ICP-MS with CE or an ultrafiltration step was developed to study the speciation of the serum protein adducts of a Ruanticancer drug under in vitro intracellular conditions [24].…”

Section: Introductionmentioning

confidence: 99%

New method for the speciation of ruthenium-based chemotherapeutics in human serum by conjoint liquid chromatography on affinity and anion-exchange monolithic disks

Martinčič

Milačić

Vidmar

et al. 2014

Journal of Chromatography A

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“…[34]), indicating the kinetically more favored binding of KP1019 towards transferrin. The influence of the cation on the binding kinetics can be assessed by comparing the rate constants for KP1019 and its sodium analogue KP1339, revealing, as expected, a similar reactivity for both Ru III compounds [57]. Under more physiological conditions, Szpunar et al studied the interaction of KP1019, KP1339, and KP418 with serum by SEC/ICP-MS [42].…”

mentioning

confidence: 96%

KP1019, A New Redox‐Active Anticancer Agent – Preclinical Development and Results of a Clinical Phase I Study in Tumor Patients

Hartinger

Jakupec

Zorbas‐Seifried

et al. 2008

Chemistry & Biodiversity

781

583

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The promising drug candidate indazolium trans-[tetrachlorobis(1H-indazole)ruthenate(III)] (KP1019) is the second Ru-based anticancer agent to enter clinical trials. In this review, which is an update of a paper from 2006 (Hartinger et al., J. Inorg. Biochem. 2006, 100, 891-904), the experimental evidence for the proposed mode of action of this coordination compound is discussed, including transport into the cell via the transferrin cycle and activation by reduction. The results of the early clinical development of KP1019 are summarized in which five out of six evaluated patients experienced disease stabilization with no severe side effects.

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Application of capillary electrophoresis–inductively coupled plasma mass spectrometry to comparative studying of the reactivity of antitumor ruthenium(III) complexes differing in the nature of counter-ion toward human serum proteins

Cited by 45 publications

References 12 publications

Mass spectrometry of peptides and proteins from human blood

Mass spectrometry of peptides and proteins from human blood

New method for the speciation of ruthenium-based chemotherapeutics in human serum by conjoint liquid chromatography on affinity and anion-exchange monolithic disks

KP1019, A New Redox‐Active Anticancer Agent – Preclinical Development and Results of a Clinical Phase I Study in Tumor Patients

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