Studies of interactions between platinum(II) complexes and some biologically relevant molecules

Petrović, Dejan; Stojimirovic, Biljana; Petrović, Biljana; Bugarčić, Živadin D.

doi:10.1016/j.bmc.2007.03.059

Cited by 42 publications

(27 citation statements)

References 40 publications

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“…Model studies under physiologically relevant conditions have conclusively shown that the kinetic preference of Pt II is for biorelevant thiols (cysteine, glutathione) rather than for 5Ј-GMP. [10,15] Methionine bound to platinum may be replaced by thiols or nucleobases, [14][15][16][17][18] whereas the Pt-cysteine bond is considered to be kinetically more inert. [10,16] Pt-sulfur adducts have been postulated to be a drug reservoir for platinum at DNA and may act as intermediates of platinum compounds and transform them into Pt-DNA adducts.…”

Section: Interest In the Development Of New Ptmentioning

confidence: 99%

“…[10,15] Methionine bound to platinum may be replaced by thiols or nucleobases, [14][15][16][17][18] whereas the Pt-cysteine bond is considered to be kinetically more inert. [10,16] Pt-sulfur adducts have been postulated to be a drug reservoir for platinum at DNA and may act as intermediates of platinum compounds and transform them into Pt-DNA adducts. [11,12] However, platinum drugs could be deactivated in reactions with cysteine-rich proteins like glutathione.…”

Section: Interest In the Development Of New Ptmentioning

confidence: 99%

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Kinetic Studies on the Reactions of Different Bifunctional Platinum(II) Complexes with Selected Nucleophiles

et al. 2010

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, where SMC = S-methyl-L-cysteine, en = ethylenediamine and dach = 1,2-diaminocyclohexane, with selected biologically important ligands, viz. guanosine-5Ј-monophosphate (5Ј-GMP), L-histidine and 1,2,4-triazole, were studied. All reactions were studied in aqueous 25 mM Hepes buffer in the presence of 5 mM NaCl at pH = 7.2 under pseudo-first-order conditions as a function of concentration at 310 K by using UV/Vis spectrophotometry. Two consecutive reaction steps, which both depend on the nucleophile concentration, were observed in

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Section: Interest In the Development Of New Ptmentioning

confidence: 99%

Section: Interest In the Development Of New Ptmentioning

confidence: 99%

Kinetic Studies on the Reactions of Different Bifunctional Platinum(II) Complexes with Selected Nucleophiles

et al. 2010

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“…Nucleophilic thiol proteins such as glutathione and metallothioneins are capable of binding to cisplatin before reaching the cellular targets. The intracellular concentration of glutathione is as high as 10 mm, and it correlates to cisplatin resistance in which 1 mol of Pt binds to 2 mol of glutathione with the rate constant of 8.45 Â 10 À 2 m À 1 s À 1 [62] [63]. Moreover, the increased levels of metallothioneins have been found in some cisplatin-resistant cells [64].…”

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confidence: 97%

Cisplatin Affects the Conformation of Apo Form, not Holo Form, of BRCA1 RING Finger Domain and Confers Thermal Stability

Atipairin

Canyuk²,

Ratanaphan³

2010

Chemistry & Biodiversity

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The breast cancer suppressor protein 1 (BRCA1) has been shown to participate in genomic integrity maintenance. Preclinical and clinical studies have recently revealed that the inactivation of BRCA1 in cancer cells leads to chemosensitivity. Approaching the BRCA1 RING protein as a potentially molecular target for a platinum-based drug might be of interest in cancer therapy. In the present study, the in vitro platination of the BRCA1 RING protein by the anticancer drug cisplatin was observed. The protein contained a preformed structure in the apo form with structural changes and resistance to limited proteolysis after Zn2+ binding. SDS-PAGE and mass-spectrometric analyses revealed that cisplatin preferentially formed monofunctional and bifunctional BRCA1 adducts. Tandem mass spectrometry (MS/MS) of the 656.29(2+) ion indicated that the ion arose from [Pt(NH3)2(OH)]+ bound to the BRCA1 peptide (111)ENNSPEHLK(119). The product-ion spectrum revealed the Pt-binding site on His117. Circular dichroism showed that the apo form, not holo form, of BRCA1 underwent more folded structural rearrangement upon cisplatin binding. Cisplatin-bound protein exhibited an enhanced thermostability by 13 degrees , resulting from the favorably intermolecular cross-links driven by the free energy. Our findings demonstrated the first conformational and thermal evidences for a direct binding of cisplatin to the BRCA1 RING domain and could raise a possibility of selectively targeted treatment of cancer with less toxicity or improved response to conventional regimens.

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“…81 Smatra se da je interakcija platine sa biomolekulima koji sadrže cistein ili metionin uzrok negativnih efekata hemoterapije, kao što su nefrotoksičnost, gastrointestinalno trovanje, ototoksičnost, neurotoksičnost i kardiotoksičnost. [82][83][84] Pt(II) ima znatno veći afinitet prema S-donorima, naročito tiolima, u odnosu na N-donore u DNK bazama. 83 Kada se platina po ulasku u ćeliju veže za neki od S-biomolekula, njena dalja subina je određena jačinom te interakcije.…”

Section: Interakcija Sa Proteinimaunclassified

“…85,86 S druge strane, interakcija sa proteinima bogatim cisteinom (glutation ili metalotionein) dovodi do inaktivacije kompleksa platine, koji mogu da zamene mesto sa azotnom bazom iz već formiranog Pt-DNK adukta ili sa tioetrom iz Pt-tioetra, formirajući stabilne Pt-tiolate. 84 Pt-glutation adukt se izbacuje iz ćelije aktivnim membranskim transportom u roku od 12 sati, pa se pretpostavlja da je glutation uzrok ćelijske rezistencije na platinu i nefrotoksičnosti. 87 Eksperimentalno se može dokazati da sa povećanjem koncentracije glutationa u ćeliji, platina u manjoj meri koordiniše za DNK.…”

Section: Interakcija Sa Proteinimaunclassified

The interaction of platinum and ruthenium complexes with pancreatic phospholipase A2 and phospholipids

Kamčeva¹

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Studies of interactions between platinum(II) complexes and some biologically relevant molecules

Cited by 42 publications

References 40 publications

Kinetic Studies on the Reactions of Different Bifunctional Platinum(II) Complexes with Selected Nucleophiles

Kinetic Studies on the Reactions of Different Bifunctional Platinum(II) Complexes with Selected Nucleophiles

Cisplatin Affects the Conformation of Apo Form, not Holo Form, of BRCA1 RING Finger Domain and Confers Thermal Stability

The interaction of platinum and ruthenium complexes with pancreatic phospholipase A2 and phospholipids

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