TY  - JOUR
AU  - Nešić, Maja D.
AU  - Dučić, Tanja
AU  - Liang, Xinyue
AU  - Algarra, Manuel
AU  - Mi, Lan
AU  - Korićanac, Lela
AU  - Žakula, Jelena
AU  - Kop, Tatjana
AU  - Bjelaković, Mira S.
AU  - Mitrović, Aleksandra D.
AU  - Gojgić-Cvijović, Gordana D.
AU  - Stepić, Milutin
AU  - Petković, Marijana
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4268
AB  - Objects of the present study are improved fullerene C60 drug carrier properties trough encapsulation by microbial polysaccharides, levan (LEV), pullulan (PUL), and their hydrophobized cholesterol-derivatives (CHL and CHP), that show better interaction with cancer cells. The zeta potential, polydispersity index, and the diameter of particles were determined, and their cytotoxicity against three cancer cell lines were tested. Biochemical changes in HeLa cells are analyzed by synchrotron radiation (SR) FTIR spectro-microscopy combined with the principal component analysis (PCA). The most significant changes occur in HeLa cells treated with LEV-C60 and correspond to the changes in the protein region, i.e. Amide Iband, and the changes in the structure of lipid bodies and membrane fluidity are evident. The highest cytotoxicity was also induced by LEV-C60. In HeLa cells, cytotoxicity could not be strictly associated with biochemical changes in lipids, proteins and nucleic acids, but these findings are significant contribution to the study of the mechanism of interaction of C60-based nanoparticles with cellular biomolecules. In conclusion, LEV, PUL, CHL, and CHP enhanced fullerene C60potential to be used as target drug delivery system with the ability to induce specific intracellular changes in HeLa cancer cells.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - SR-FTIR spectro-microscopic interaction study of biochemical changes in HeLa cells induced by Levan-C60, Pullulan-C60, and their cholesterol-derivatives
VL  - 165
IS  - B
SP  - 2541
EP  - 2549
DO  - 10.1016/j.ijbiomac.2020.10.141
ER  - 

@article{
author = "Nešić, Maja D. and Dučić, Tanja and Liang, Xinyue and Algarra, Manuel and Mi, Lan and Korićanac, Lela and Žakula, Jelena and Kop, Tatjana and Bjelaković, Mira S. and Mitrović, Aleksandra D. and Gojgić-Cvijović, Gordana D. and Stepić, Milutin and Petković, Marijana",
year = "2020",
abstract = "Objects of the present study are improved fullerene C60 drug carrier properties trough encapsulation by microbial polysaccharides, levan (LEV), pullulan (PUL), and their hydrophobized cholesterol-derivatives (CHL and CHP), that show better interaction with cancer cells. The zeta potential, polydispersity index, and the diameter of particles were determined, and their cytotoxicity against three cancer cell lines were tested. Biochemical changes in HeLa cells are analyzed by synchrotron radiation (SR) FTIR spectro-microscopy combined with the principal component analysis (PCA). The most significant changes occur in HeLa cells treated with LEV-C60 and correspond to the changes in the protein region, i.e. Amide Iband, and the changes in the structure of lipid bodies and membrane fluidity are evident. The highest cytotoxicity was also induced by LEV-C60. In HeLa cells, cytotoxicity could not be strictly associated with biochemical changes in lipids, proteins and nucleic acids, but these findings are significant contribution to the study of the mechanism of interaction of C60-based nanoparticles with cellular biomolecules. In conclusion, LEV, PUL, CHL, and CHP enhanced fullerene C60potential to be used as target drug delivery system with the ability to induce specific intracellular changes in HeLa cancer cells.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "SR-FTIR spectro-microscopic interaction study of biochemical changes in HeLa cells induced by Levan-C60, Pullulan-C60, and their cholesterol-derivatives",
volume = "165",
number = "B",
pages = "2541-2549",
doi = "10.1016/j.ijbiomac.2020.10.141"
}

Nešić, M. D., Dučić, T., Liang, X., Algarra, M., Mi, L., Korićanac, L., Žakula, J., Kop, T., Bjelaković, M. S., Mitrović, A. D., Gojgić-Cvijović, G. D., Stepić, M.,& Petković, M.. (2020). SR-FTIR spectro-microscopic interaction study of biochemical changes in HeLa cells induced by Levan-C60, Pullulan-C60, and their cholesterol-derivatives. in International Journal of Biological Macromolecules
Elsevier., 165(B), 2541-2549.
https://doi.org/10.1016/j.ijbiomac.2020.10.141

Nešić MD, Dučić T, Liang X, Algarra M, Mi L, Korićanac L, Žakula J, Kop T, Bjelaković MS, Mitrović AD, Gojgić-Cvijović GD, Stepić M, Petković M. SR-FTIR spectro-microscopic interaction study of biochemical changes in HeLa cells induced by Levan-C60, Pullulan-C60, and their cholesterol-derivatives. in International Journal of Biological Macromolecules. 2020;165(B):2541-2549.
doi:10.1016/j.ijbiomac.2020.10.141 .

Nešić, Maja D., Dučić, Tanja, Liang, Xinyue, Algarra, Manuel, Mi, Lan, Korićanac, Lela, Žakula, Jelena, Kop, Tatjana, Bjelaković, Mira S., Mitrović, Aleksandra D., Gojgić-Cvijović, Gordana D., Stepić, Milutin, Petković, Marijana, "SR-FTIR spectro-microscopic interaction study of biochemical changes in HeLa cells induced by Levan-C60, Pullulan-C60, and their cholesterol-derivatives" in International Journal of Biological Macromolecules, 165, no. B (2020):2541-2549,
https://doi.org/10.1016/j.ijbiomac.2020.10.141 . .

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 . .

TY  - DATA
AU  - Dimkić, Ivica
AU  - Stanković, Slaviša
AU  - Nišavić, Marija
AU  - Petković, Marijana
AU  - Ristivojević, Petar
AU  - Fira, Đorđe
AU  - Berić, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3113
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - Supplementary data for article: Dimkic, I.; Stankovic, S.; Nišavic, M.; Petkovic, M.; Ristivojevic, P.; Fira, D.; Beric, T. The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. Frontiers in Microbiology 2017, 8 (MAY). https://doi.org/10.3389/fmicb.2017.00925
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3113
ER  - 

@misc{
author = "Dimkić, Ivica and Stanković, Slaviša and Nišavić, Marija and Petković, Marijana and Ristivojević, Petar and Fira, Đorđe and Berić, Tanja",
year = "2017",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "Supplementary data for article: Dimkic, I.; Stankovic, S.; Nišavic, M.; Petkovic, M.; Ristivojevic, P.; Fira, D.; Beric, T. The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. Frontiers in Microbiology 2017, 8 (MAY). https://doi.org/10.3389/fmicb.2017.00925",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3113"
}

Dimkić, I., Stanković, S., Nišavić, M., Petković, M., Ristivojević, P., Fira, Đ.,& Berić, T.. (2017). Supplementary data for article: Dimkic, I.; Stankovic, S.; Nišavic, M.; Petkovic, M.; Ristivojevic, P.; Fira, D.; Beric, T. The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. Frontiers in Microbiology 2017, 8 (MAY). https://doi.org/10.3389/fmicb.2017.00925. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne..
https://hdl.handle.net/21.15107/rcub_cherry_3113

Dimkić I, Stanković S, Nišavić M, Petković M, Ristivojević P, Fira Đ, Berić T. Supplementary data for article: Dimkic, I.; Stankovic, S.; Nišavic, M.; Petkovic, M.; Ristivojevic, P.; Fira, D.; Beric, T. The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. Frontiers in Microbiology 2017, 8 (MAY). https://doi.org/10.3389/fmicb.2017.00925. in Frontiers in Microbiology. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_3113 .

Dimkić, Ivica, Stanković, Slaviša, Nišavić, Marija, Petković, Marijana, Ristivojević, Petar, Fira, Đorđe, Berić, Tanja, "Supplementary data for article: Dimkic, I.; Stankovic, S.; Nišavic, M.; Petkovic, M.; Ristivojevic, P.; Fira, D.; Beric, T. The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. Frontiers in Microbiology 2017, 8 (MAY). https://doi.org/10.3389/fmicb.2017.00925" in Frontiers in Microbiology (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3113 .

TY  - JOUR
AU  - Dimkić, Ivica
AU  - Stanković, Slaviša
AU  - Nišavić, Marija
AU  - Petković, Marijana
AU  - Ristivojević, Petar
AU  - Fira, Đorđe
AU  - Berić, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2463
AB  - In this study the efficacy of two different methods for extracting lipopeptides produced by five Bacillus strains-ethyl acetate extraction, and acid precipitation followed by methanol extraction-was investigated using mass spectrometry. High performance thin layer chromatography (HPTLC) was also used for the simultaneous separation of complex mixtures of lipopeptide extracts and for the determination of antimicrobial activity of their components. The mass spectra clearly showed well-resolved groups of peaks corresponding to different lipopeptide families (kurstakins, iturins, surfactins, and fengycins). The ethyl acetate extracts produced the most favorable results. The extracts of SS-12.6, SS-13.1, and SS-38.4 showed the highest inhibition zones. An iturin analog is responsible for the inhibition of Xanthomonas arboricola and Pseudomonas syringae phytopathogenic strains. HPTLC bioautography effectively identified the active compounds from a mixture of lipopeptide extracts, proving in situ its potential for use in direct detection and determination of antimicrobials. In the test of potential synergism among individual extracts used in different mixtures, stronger antimicrobial effects were not observed. Biochemical and phylogenetic analysis clustered isolates SS-12.6, SS-13.1, SS-27.2, and SS-38.4 together with Bacillus amyloliquefaciens, while SS-10.7 was more closely related to Bacillus pumilus.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains
VL  - 8
DO  - 10.3389/fmicb.2017.00925
ER  - 

@article{
author = "Dimkić, Ivica and Stanković, Slaviša and Nišavić, Marija and Petković, Marijana and Ristivojević, Petar and Fira, Đorđe and Berić, Tanja",
year = "2017",
abstract = "In this study the efficacy of two different methods for extracting lipopeptides produced by five Bacillus strains-ethyl acetate extraction, and acid precipitation followed by methanol extraction-was investigated using mass spectrometry. High performance thin layer chromatography (HPTLC) was also used for the simultaneous separation of complex mixtures of lipopeptide extracts and for the determination of antimicrobial activity of their components. The mass spectra clearly showed well-resolved groups of peaks corresponding to different lipopeptide families (kurstakins, iturins, surfactins, and fengycins). The ethyl acetate extracts produced the most favorable results. The extracts of SS-12.6, SS-13.1, and SS-38.4 showed the highest inhibition zones. An iturin analog is responsible for the inhibition of Xanthomonas arboricola and Pseudomonas syringae phytopathogenic strains. HPTLC bioautography effectively identified the active compounds from a mixture of lipopeptide extracts, proving in situ its potential for use in direct detection and determination of antimicrobials. In the test of potential synergism among individual extracts used in different mixtures, stronger antimicrobial effects were not observed. Biochemical and phylogenetic analysis clustered isolates SS-12.6, SS-13.1, SS-27.2, and SS-38.4 together with Bacillus amyloliquefaciens, while SS-10.7 was more closely related to Bacillus pumilus.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains",
volume = "8",
doi = "10.3389/fmicb.2017.00925"
}

Dimkić, I., Stanković, S., Nišavić, M., Petković, M., Ristivojević, P., Fira, Đ.,& Berić, T.. (2017). The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 8.
https://doi.org/10.3389/fmicb.2017.00925

Dimkić I, Stanković S, Nišavić M, Petković M, Ristivojević P, Fira Đ, Berić T. The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains. in Frontiers in Microbiology. 2017;8.
doi:10.3389/fmicb.2017.00925 .

Dimkić, Ivica, Stanković, Slaviša, Nišavić, Marija, Petković, Marijana, Ristivojević, Petar, Fira, Đorđe, Berić, Tanja, "The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains" in Frontiers in Microbiology, 8 (2017),
https://doi.org/10.3389/fmicb.2017.00925 . .

TY  - JOUR
AU  - Dimkić, Ivica
AU  - Stanković, Slaviša
AU  - Nišavić, Marija
AU  - Petković, Marijana
AU  - Ristivojević, Petar
AU  - Fira, Đorđe
AU  - Berić, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2497
AB  - In the original article, there was an error. Due to the oversight, a technical error was made in some parts of first two sentences, in the section Bacterial Isolates Used in Bioautography Assay. The corrections include the isolates code (IZB for the Xanthomonas strains), and the origin of the collection (Institute for Plant Protection and Environment, Belgrade, Serbia instead Laboratory of Microbiology, Faculty of Biology, University of Belgrade). The corrected paragraph appears below: The antibacterial activity of the Bacillus spp. extracts was measured against phytopathogenic bacteria Pseudomonas syringae pv. aptata (P16) isolated from sugar beets, and Xanthomonas arboricola pv. juglandis (IZB 301, IZB 311, and IZB 320; hereinafter referred to: 301, 311, and 320), originating from walnut trees. The phytopathogenic strains were previously identified and belong to the collection of the Institute for Plant Protection and Environment, Belgrade, Serbia. The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. © 2017 Dimkić, Stanković, Nišavić, Petković, Ristivojević, Fira and Berić.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Microbiology
T1  - The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017)
VL  - 8
DO  - 10.3389/fmicb.2017.01500
ER  - 

@article{
author = "Dimkić, Ivica and Stanković, Slaviša and Nišavić, Marija and Petković, Marijana and Ristivojević, Petar and Fira, Đorđe and Berić, Tanja",
year = "2017",
abstract = "In the original article, there was an error. Due to the oversight, a technical error was made in some parts of first two sentences, in the section Bacterial Isolates Used in Bioautography Assay. The corrections include the isolates code (IZB for the Xanthomonas strains), and the origin of the collection (Institute for Plant Protection and Environment, Belgrade, Serbia instead Laboratory of Microbiology, Faculty of Biology, University of Belgrade). The corrected paragraph appears below: The antibacterial activity of the Bacillus spp. extracts was measured against phytopathogenic bacteria Pseudomonas syringae pv. aptata (P16) isolated from sugar beets, and Xanthomonas arboricola pv. juglandis (IZB 301, IZB 311, and IZB 320; hereinafter referred to: 301, 311, and 320), originating from walnut trees. The phytopathogenic strains were previously identified and belong to the collection of the Institute for Plant Protection and Environment, Belgrade, Serbia. The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. © 2017 Dimkić, Stanković, Nišavić, Petković, Ristivojević, Fira and Berić.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Microbiology",
title = "The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017)",
volume = "8",
doi = "10.3389/fmicb.2017.01500"
}

Dimkić, I., Stanković, S., Nišavić, M., Petković, M., Ristivojević, P., Fira, Đ.,& Berić, T.. (2017). The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017). in Frontiers in Microbiology
Frontiers Media Sa, Lausanne., 8.
https://doi.org/10.3389/fmicb.2017.01500

Dimkić I, Stanković S, Nišavić M, Petković M, Ristivojević P, Fira Đ, Berić T. The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017). in Frontiers in Microbiology. 2017;8.
doi:10.3389/fmicb.2017.01500 .

Dimkić, Ivica, Stanković, Slaviša, Nišavić, Marija, Petković, Marijana, Ristivojević, Petar, Fira, Đorđe, Berić, Tanja, "The Profile and Antimicrobial Activity of Bacillus Lipopeptide Extracts of Five Potential Biocontrol Strains (vol 8, pg 925, 2017)" in Frontiers in Microbiology, 8 (2017),
https://doi.org/10.3389/fmicb.2017.01500 . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Theisgen, Stephan
AU  - Scheidt, Holger A.
AU  - Petković, Marijana
AU  - Huster, Daniel
AU  - Vujčić, Zoran
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1245
AB  - Understanding the effect of surface charge on the stability of proteins is one prerequisite for "tailoring" proteins with increased thermal stability. Here, we investigated the origin of the altered thermal stability observed between the four recently isolated isoforms (EINV1-EINV4) of external invertase. External invertase from yeast Saccharomyces cerevisiae, a homodimeric glycoprotein, represents a widely used model for studying the influence of the glyco component on protein stability. The stability of the four isoforms of invertase decreases from EINV1 to EINV4, which is accompanied by an increase in negative surface charge density. Mass spectrometry analysis revealed that the isoforms share identical protein parts indicating that the differences in stability are the result of post-translational modifications. P-31 NMR analysis revealed that the isoforms contain negatively charged phosphate groups in diester and monoester forms attached to the glycan part. The total amount of phosphate bound to the polymannan component varies between the different isoforms. These results, together with the analysis of the amount of polymannan components, show that negative surface charge density does not entirely depend on the amount of phosphate but rather on its distribution. This suggests that charged groups bound to the glyco-component of a protein can influence the stability of glycoproteins. (C) 2011 Elsevier Masson SAS. All rights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - Biochimie
T1  - The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density
VL  - 94
IS  - 2
SP  - 510
EP  - 515
DO  - 10.1016/j.biochi.2011.08.020
ER  - 

@article{
author = "Anđelković, Uroš and Theisgen, Stephan and Scheidt, Holger A. and Petković, Marijana and Huster, Daniel and Vujčić, Zoran",
year = "2012",
abstract = "Understanding the effect of surface charge on the stability of proteins is one prerequisite for "tailoring" proteins with increased thermal stability. Here, we investigated the origin of the altered thermal stability observed between the four recently isolated isoforms (EINV1-EINV4) of external invertase. External invertase from yeast Saccharomyces cerevisiae, a homodimeric glycoprotein, represents a widely used model for studying the influence of the glyco component on protein stability. The stability of the four isoforms of invertase decreases from EINV1 to EINV4, which is accompanied by an increase in negative surface charge density. Mass spectrometry analysis revealed that the isoforms share identical protein parts indicating that the differences in stability are the result of post-translational modifications. P-31 NMR analysis revealed that the isoforms contain negatively charged phosphate groups in diester and monoester forms attached to the glycan part. The total amount of phosphate bound to the polymannan component varies between the different isoforms. These results, together with the analysis of the amount of polymannan components, show that negative surface charge density does not entirely depend on the amount of phosphate but rather on its distribution. This suggests that charged groups bound to the glyco-component of a protein can influence the stability of glycoproteins. (C) 2011 Elsevier Masson SAS. All rights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "Biochimie",
title = "The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density",
volume = "94",
number = "2",
pages = "510-515",
doi = "10.1016/j.biochi.2011.08.020"
}

Anđelković, U., Theisgen, S., Scheidt, H. A., Petković, M., Huster, D.,& Vujčić, Z.. (2012). The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density. in Biochimie
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris., 94(2), 510-515.
https://doi.org/10.1016/j.biochi.2011.08.020

Anđelković U, Theisgen S, Scheidt HA, Petković M, Huster D, Vujčić Z. The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density. in Biochimie. 2012;94(2):510-515.
doi:10.1016/j.biochi.2011.08.020 .

Anđelković, Uroš, Theisgen, Stephan, Scheidt, Holger A., Petković, Marijana, Huster, Daniel, Vujčić, Zoran, "The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density" in Biochimie, 94, no. 2 (2012):510-515,
https://doi.org/10.1016/j.biochi.2011.08.020 . .

TY  - CONF
AU  - Jovanović, Ivana
AU  - Petković, Marijana
AU  - Vujčić, Zoran
AU  - Jordović, Branka
AU  - Ignjatović, Nenad
AU  - Uskoković, Dragan P.
PY  - 2007
UR  - http://dais.sanu.ac.rs/123456789/319
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2781
AB  - Poster presented at the 9th Conference of the Yugoslav Materials Research Society - YUCOMAT 2007, Herceg Novi, Crna Gora, September 10-14, 2007.
T1  - PDLLA Microparticles Containing BSA: Effect of Formulation Variables on Size Distribution
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2781
ER  - 

@conference{
author = "Jovanović, Ivana and Petković, Marijana and Vujčić, Zoran and Jordović, Branka and Ignjatović, Nenad and Uskoković, Dragan P.",
year = "2007",
abstract = "Poster presented at the 9th Conference of the Yugoslav Materials Research Society - YUCOMAT 2007, Herceg Novi, Crna Gora, September 10-14, 2007.",
title = "PDLLA Microparticles Containing BSA: Effect of Formulation Variables on Size Distribution",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2781"
}

Jovanović, I., Petković, M., Vujčić, Z., Jordović, B., Ignjatović, N.,& Uskoković, D. P.. (2007). PDLLA Microparticles Containing BSA: Effect of Formulation Variables on Size Distribution. .
https://hdl.handle.net/21.15107/rcub_cherry_2781

Jovanović I, Petković M, Vujčić Z, Jordović B, Ignjatović N, Uskoković DP. PDLLA Microparticles Containing BSA: Effect of Formulation Variables on Size Distribution. 2007;.
https://hdl.handle.net/21.15107/rcub_cherry_2781 .

Jovanović, Ivana, Petković, Marijana, Vujčić, Zoran, Jordović, Branka, Ignjatović, Nenad, Uskoković, Dragan P., "PDLLA Microparticles Containing BSA: Effect of Formulation Variables on Size Distribution" (2007),
https://hdl.handle.net/21.15107/rcub_cherry_2781 .