Carboplatin binding to histidine

Tanley, S.W.M.; Diederichs, Kay; Kroon-Batenburg, Loes M. L.; Levy, Colin; Schreurs, Antoine M. M.; Helliwell, John R.

doi:10.1107/s2053230x14016161

Cited by 38 publications

(49 citation statements)

References 33 publications

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“…4A and B and Fig. As expected on the basis of the comparison between the structure of HEWL-cisplatin 20 and that of HEWL-oxaliplatin, 21 the former binding site, i.e. As expected on the basis of the comparison between the structure of HEWL-cisplatin 20 and that of HEWL-oxaliplatin, 21 the former binding site, i.e.…”

Section: Crystallographysupporting

confidence: 60%

“…[7][8][9] To better understand the pharmacological profiles of cisplatin, carboplatin and oxaliplatin it is imperative to study the mechanism by which these Pt drugs interact with proteins. [18][19][20][21][22][23] Notably, this well-behaved enzyme has been studied in complexes with cisplatin, [18][19][20] carboplatin, 20 oxaliplatin, 21 cis-PtI 2 (NH 3 ) 2 22 and trans-Pt derivatives. 10,12,14,15 Electrospray mass spectrometry (ESI MS) measurements 14,[16][17][18] and crystallographic studies 18-25 on small model proteins allowed a number of details on the protein metalation process to be obtained.…”

Section: Introductionmentioning

confidence: 99%

“…10,12,14,15 Electrospray mass spectrometry (ESI MS) measurements 14,[16][17][18] and crystallographic studies 18-25 on small model proteins allowed a number of details on the protein metalation process to be obtained. 20 In particular, upon reaction between cisplatin and HEWL, platination occurs at the level of His15, with a cis-Pt(NH 3 ) 2 2+ fragment bound to the protein surface. [18][19][20][21][22][23] Notably, this well-behaved enzyme has been studied in complexes with cisplatin, [18][19][20] carboplatin, 20 oxaliplatin, 21 cis-PtI 2 (NH 3 ) 2 22 and trans-Pt derivatives.…”

Section: Introductionmentioning

confidence: 99%

“…In this framework, hen egg white lysozyme (HEWL) has been extensively used as a model protein. [18][19][20] On the other hand, the reaction between HEWL and oxaliplatin leads to the formation of a complex with the Pt(dach) 2+ moiety bound to Asp119. 23 It was recently shown that HEWL is able to bind cisplatin and oxaliplatin in two distinct binding sites, 21 whereas cisplatin and carboplatin compete for the same residue side chain.…”

Section: Introductionmentioning

confidence: 99%

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Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme

et al. 2015

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The model protein hen egg white lysozyme was challenged with oxaliplatin and cisplatin. ESI mass spectrometry, surface plasmon resonance and thermal shift analyses demonstrate the formation of a bis-platinum adduct, though in very small amounts. Crystals of the bis-platinum adduct were obtained using two different preparations and the X-ray structures were solved at 1.85 Å and 1.95 Å resolution. Overall, the obtained data point out that, under the analyzed conditions, the two Pt drugs have similar affinities for the protein, but bind on its surface at two non-overlapping sites. In other words, these two drugs manifest a significantly different reactivity with this model protein and do not compete for the same protein binding sites.

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Section: Crystallographysupporting

confidence: 60%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme

et al. 2015

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“…These two proteins have been often used to study protein modifications induced by metal based drugs (Santos-Silva et al 2011;Helliwell and Tanley 2013;Messori et al 2013a, b;Messori et al 2014a, b;Tanley et al 2012a, b;Tanley et al 2013Tanley et al , 2014Messori and Merlino 2014a, b).…”

Section: Introductionmentioning

confidence: 96%

Structural evidences for a secondary gold binding site in the hydrophobic box of lysozyme

et al. 2015

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A new crystal structure is reported here for the adduct formed in the reaction between NH4 [Au(Sac)2], AuSac2, a cytotoxic homoleptic gold(I) complex with the saccharinate ligand, and the model protein hen egg white lysozyme. To produce this adduct, AuSac2 breaks down and releases both saccharinate ligands. The resulting Au(I) ions bind the protein to ND1 and NE2 atoms of His15 but also to SD atom of the zero-solvent accessible Met105 side chain, which is located in the protein hydrophobic box. The unexpected existence of this secondary gold(I) binding site is confirmed by spectroscopic and spectrometric measurements in solution.

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A novel and fully validated hydrophilic interaction liquid chromatography with tandem mass spectrometry method for the determination of intact carboplatin in human plasma

Ren

Qin

Fan

et al. 2018

Separation Science Plus

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Carboplatin is an anticancer drug widely used to treat a variety of cancers. However, a simple, sensitive and rapid method for the quantitation of intact carboplatin is still absence for therapeutic drug monitoring or clinical trials. In this work, a rapid, universal, and reliable hydrophilic interaction liquid chromatography with tandem mass spectrometry method for the determination of intact carboplatin in human plasma was developed and fully validated. Carboplatin was extracted from human plasma by simple protein precipitation with acetonitrile. A good chromatographic separation of carboplatin was achieved on a Waters XBridge HILIC column (2.1 × 150 mm, 3.5 μm), with the analytical time 5.5 min for one sample. The linearity range of the assay was from 10 to 2000 ng/mL. The method was linear (r2 > 0.9989), accurate (<6% bias, 12% bias at LOQ) and precise (intra‐day and inter‐day precision of <3% coefficient of variation). The stability of intact carboplatin in human plasma with three different anticoagulants was assessed in this study. Furthermore, the matrix effect of hemolysis and hyperlipidemic samples was also evaluated for the first time. This work made the routine determination of intact carboplatin feasible and universal in clinical practice.

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Carboplatin binding to histidine

Abstract: An X-ray crystal structure showing the binding of purely carboplatin to histidine in a model protein has finally been obtained. This required extensive crystallization trials and various novel crystal structure analyses.

Cited by 38 publications

References 33 publications

Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme

Oxaliplatin vs. cisplatin: competition experiments on their binding to lysozyme

Structural evidences for a secondary gold binding site in the hydrophobic box of lysozyme

A novel and fully validated hydrophilic interaction liquid chromatography with tandem mass spectrometry method for the determination of intact carboplatin in human plasma

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