TY  - JOUR
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3243
AB  - Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.
PB  - Royal Soc Chemistry, Cambridge
T2  - Metallomics
T1  - Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins
VL  - 10
IS  - 4
SP  - 587
EP  - 594
DO  - 10.1039/c7mt00330g
ER  - 

@article{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
abstract = "Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Metallomics",
title = "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins",
volume = "10",
number = "4",
pages = "587-594",
doi = "10.1039/c7mt00330g"
}

Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M.. (2018). Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics
Royal Soc Chemistry, Cambridge., 10(4), 587-594.
https://doi.org/10.1039/c7mt00330g

Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics. 2018;10(4):587-594.
doi:10.1039/c7mt00330g .

Nišavić, Marija, Janjić, Goran V., Hozić, Amela, Petković, Marijana, Milčić, Miloš K., Vujčić, Zoran, Cindrić, Mario, "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins" in Metallomics, 10, no. 4 (2018):587-594,
https://doi.org/10.1039/c7mt00330g . .

TY  - DATA
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3244
PB  - Royal Soc Chemistry, Cambridge
T2  - Metallomics
T1  - Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3244
ER  - 

@misc{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Metallomics",
title = "Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3244"
}

Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M.. (2018). Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g. in Metallomics
Royal Soc Chemistry, Cambridge..
https://hdl.handle.net/21.15107/rcub_cherry_3244

Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g. in Metallomics. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3244 .

Nišavić, Marija, Janjić, Goran V., Hozić, Amela, Petković, Marijana, Milčić, Miloš K., Vujčić, Zoran, Cindrić, Mario, "Supplementary material for the article: Nišavić, M.; Janjić, G. V.; Hozić, A.; Petković, M.; Milčić, M. K.; Vujčić, Z.; Cindrić, M. Positive and Negative Nano-Electrospray Mass Spectrometry of Ruthenated Serum Albumin Supported by Docking Studies: An Integrated Approach towards Defining Metallodrug Binding Sites on Proteins. Metallomics 2018, 10 (4), 587–594. https://doi.org/10.1039/c7mt00330g" in Metallomics (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3244 .

TY  - JOUR
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2134
AB  - Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.
PB  - Royal Soc Chemistry, Cambridge
T2  - Metallomics
T1  - Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins
VL  - 10
IS  - 4
SP  - 587
EP  - 594
DO  - 10.1039/c7mt00330g
ER  - 

@article{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
abstract = "Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Metallomics",
title = "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins",
volume = "10",
number = "4",
pages = "587-594",
doi = "10.1039/c7mt00330g"
}

Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M.. (2018). Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics
Royal Soc Chemistry, Cambridge., 10(4), 587-594.
https://doi.org/10.1039/c7mt00330g

Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics. 2018;10(4):587-594.
doi:10.1039/c7mt00330g .

Nišavić, Marija, Janjić, Goran V., Hozić, Amela, Petković, Marijana, Milčić, Miloš K., Vujčić, Zoran, Cindrić, Mario, "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins" in Metallomics, 10, no. 4 (2018):587-594,
https://doi.org/10.1039/c7mt00330g . .