TY  - JOUR
AU  - Novaković, Irena T.
AU  - Anđelković, Uroš
AU  - Zlatović, Mario
AU  - Gasic, Miroslav J.
AU  - Sladić, Dušan
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1241
AB  - A conjugate of lysozyme with avarone, a bioactive sesquiterpene quinone of marine origin, and its three derivatives were synthesized. MALDI TOF mass spectral analysis and tryptic digestion showed that the only residue in lysozyme that was modified by all derivatives was lysine 97. The identity of the residue was in full correlation with the prediction obtained by molecular modeling. All bioconjugates preserved most of the enzymatic activity of lysozyme. The melting point of the conjugates was slightly increased in comparison to lysozyme, indicating a slight stabilization of structure. The antibacterial activity of all the conjugates to both Gram positive and Gram negative bacteria was stronger than the activity of either lysozyme or the quinones, the MIC values being in low micromolar range for some conjugates.
PB  - Amer Chemical Soc, Washington
T2  - Bioconjugate Chemistry
T1  - Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives
VL  - 23
IS  - 1
SP  - 57
EP  - 65
DO  - 10.1021/bc200330m
ER  - 

@article{
author = "Novaković, Irena T. and Anđelković, Uroš and Zlatović, Mario and Gasic, Miroslav J. and Sladić, Dušan",
year = "2012",
abstract = "A conjugate of lysozyme with avarone, a bioactive sesquiterpene quinone of marine origin, and its three derivatives were synthesized. MALDI TOF mass spectral analysis and tryptic digestion showed that the only residue in lysozyme that was modified by all derivatives was lysine 97. The identity of the residue was in full correlation with the prediction obtained by molecular modeling. All bioconjugates preserved most of the enzymatic activity of lysozyme. The melting point of the conjugates was slightly increased in comparison to lysozyme, indicating a slight stabilization of structure. The antibacterial activity of all the conjugates to both Gram positive and Gram negative bacteria was stronger than the activity of either lysozyme or the quinones, the MIC values being in low micromolar range for some conjugates.",
publisher = "Amer Chemical Soc, Washington",
journal = "Bioconjugate Chemistry",
title = "Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives",
volume = "23",
number = "1",
pages = "57-65",
doi = "10.1021/bc200330m"
}

Novaković, I. T., Anđelković, U., Zlatović, M., Gasic, M. J.,& Sladić, D.. (2012). Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives. in Bioconjugate Chemistry
Amer Chemical Soc, Washington., 23(1), 57-65.
https://doi.org/10.1021/bc200330m

Novaković IT, Anđelković U, Zlatović M, Gasic MJ, Sladić D. Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives. in Bioconjugate Chemistry. 2012;23(1):57-65.
doi:10.1021/bc200330m .

Novaković, Irena T., Anđelković, Uroš, Zlatović, Mario, Gasic, Miroslav J., Sladić, Dušan, "Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives" in Bioconjugate Chemistry, 23, no. 1 (2012):57-65,
https://doi.org/10.1021/bc200330m . .

TY  - JOUR
AU  - Novaković, Irena T.
AU  - Anđelković, Uroš
AU  - Zlatović, Mario
AU  - Gasic, Miroslav J.
AU  - Sladić, Dušan
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2786
AB  - A conjugate of lysozyme with avarone, a bioactive sesquiterpene quinone of marine origin, and its three derivatives were synthesized. MALDI TOF mass spectral analysis and tryptic digestion showed that the only residue in lysozyme that was modified by all derivatives was lysine 97. The identity of the residue was in full correlation with the prediction obtained by molecular modeling. All bioconjugates preserved most of the enzymatic activity of lysozyme. The melting point of the conjugates was slightly increased in comparison to lysozyme, indicating a slight stabilization of structure. The antibacterial activity of all the conjugates to both Gram positive and Gram negative bacteria was stronger than the activity of either lysozyme or the quinones, the MIC values being in low micromolar range for some conjugates.
PB  - Amer Chemical Soc, Washington
T2  - Bioconjugate Chemistry
T1  - Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives
VL  - 23
IS  - 1
SP  - 57
EP  - 65
DO  - 10.1021/bc200330m
ER  - 

@article{
author = "Novaković, Irena T. and Anđelković, Uroš and Zlatović, Mario and Gasic, Miroslav J. and Sladić, Dušan",
year = "2012",
abstract = "A conjugate of lysozyme with avarone, a bioactive sesquiterpene quinone of marine origin, and its three derivatives were synthesized. MALDI TOF mass spectral analysis and tryptic digestion showed that the only residue in lysozyme that was modified by all derivatives was lysine 97. The identity of the residue was in full correlation with the prediction obtained by molecular modeling. All bioconjugates preserved most of the enzymatic activity of lysozyme. The melting point of the conjugates was slightly increased in comparison to lysozyme, indicating a slight stabilization of structure. The antibacterial activity of all the conjugates to both Gram positive and Gram negative bacteria was stronger than the activity of either lysozyme or the quinones, the MIC values being in low micromolar range for some conjugates.",
publisher = "Amer Chemical Soc, Washington",
journal = "Bioconjugate Chemistry",
title = "Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives",
volume = "23",
number = "1",
pages = "57-65",
doi = "10.1021/bc200330m"
}

Novaković, I. T., Anđelković, U., Zlatović, M., Gasic, M. J.,& Sladić, D.. (2012). Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives. in Bioconjugate Chemistry
Amer Chemical Soc, Washington., 23(1), 57-65.
https://doi.org/10.1021/bc200330m

Novaković IT, Anđelković U, Zlatović M, Gasic MJ, Sladić D. Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives. in Bioconjugate Chemistry. 2012;23(1):57-65.
doi:10.1021/bc200330m .

Novaković, Irena T., Anđelković, Uroš, Zlatović, Mario, Gasic, Miroslav J., Sladić, Dušan, "Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives" in Bioconjugate Chemistry, 23, no. 1 (2012):57-65,
https://doi.org/10.1021/bc200330m . .

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 . .