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  - THES
AU  - Nišavić, Marija
PY  - 2017
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=5597
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:17106/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=49836815
UR  - http://nardus.mpn.gov.rs/123456789/9177
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2748
AB  - Ova disertacija se bavi ispitivanjem interakcija tri potencijalna antitumorska kompleksa Ru(II) opšte formule mer-[Ru(Cl-tpy)(N-N)Cl]Cl (Cl-tpy - 4′-hloro-2,2′:6′,2″-terpiridin; N-N - 1,2-diaminoetan (en), 1,2-diaminocikloheksan (dach) ili 2,2′-bipiridin (bipy)) sa transportnim proteinima seruma, humanim serum albuminom (HSA) i transferinom (Tf). Odabrani kompleksi Ru(II) pripadaju novoj klasi terpiridinskih kompleksa meridionalne geometrije, koji pokazuju visoku rastvorljivost u vodi. Do sada je u literaturi pokazana sposobnost ovih kompleksa da grade monofukcionalne adukte sa derivatima guanina, istiĉući njihov potencijal za vezivanje za DNK molekul. MeĊutim, interakcije sa proteinima do sada nisu ispitane. Kako se antikancerski agensi na bazi metala u organizam unose intravenozno, vezivanje kompleksa za transportne proteine seruma je izuzetno vaţno jer moţe znaĉajno uticati na njihovu biodistribuciju i efikasnost...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Ispitivanje interakcija terpiridinskih kompleksa rutenijuma(II) sa transportnim proteinima seruma
UR  - https://hdl.handle.net/21.15107/rcub_nardus_9177
ER  - 

@phdthesis{
author = "Nišavić, Marija",
year = "2017",
abstract = "Ova disertacija se bavi ispitivanjem interakcija tri potencijalna antitumorska kompleksa Ru(II) opšte formule mer-[Ru(Cl-tpy)(N-N)Cl]Cl (Cl-tpy - 4′-hloro-2,2′:6′,2″-terpiridin; N-N - 1,2-diaminoetan (en), 1,2-diaminocikloheksan (dach) ili 2,2′-bipiridin (bipy)) sa transportnim proteinima seruma, humanim serum albuminom (HSA) i transferinom (Tf). Odabrani kompleksi Ru(II) pripadaju novoj klasi terpiridinskih kompleksa meridionalne geometrije, koji pokazuju visoku rastvorljivost u vodi. Do sada je u literaturi pokazana sposobnost ovih kompleksa da grade monofukcionalne adukte sa derivatima guanina, istiĉući njihov potencijal za vezivanje za DNK molekul. MeĊutim, interakcije sa proteinima do sada nisu ispitane. Kako se antikancerski agensi na bazi metala u organizam unose intravenozno, vezivanje kompleksa za transportne proteine seruma je izuzetno vaţno jer moţe znaĉajno uticati na njihovu biodistribuciju i efikasnost...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Ispitivanje interakcija terpiridinskih kompleksa rutenijuma(II) sa transportnim proteinima seruma",
url = "https://hdl.handle.net/21.15107/rcub_nardus_9177"
}

Nišavić, M.. (2017). Ispitivanje interakcija terpiridinskih kompleksa rutenijuma(II) sa transportnim proteinima seruma. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
https://hdl.handle.net/21.15107/rcub_nardus_9177

Nišavić M. Ispitivanje interakcija terpiridinskih kompleksa rutenijuma(II) sa transportnim proteinima seruma. in Универзитет у Београду. 2017;.
https://hdl.handle.net/21.15107/rcub_nardus_9177 .

Nišavić, Marija, "Ispitivanje interakcija terpiridinskih kompleksa rutenijuma(II) sa transportnim proteinima seruma" in Универзитет у Београду (2017),
https://hdl.handle.net/21.15107/rcub_nardus_9177 .

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 . .