CER - Central Repository
Institute of Chemistry, Technology and Metallurgy
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrillic)
    • Serbian (Latin)
  • Login
View Item 
  •   CER
  • IHTM
  • Radovi istraživača / Researchers' publications
  • View Item
  •   CER
  • IHTM
  • Radovi istraživača / Researchers' publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives

Thumbnail
2012
1003.pdf (1.725Mb)
Authors
Novaković, Irena
Anđelković, Uroš
Zlatović, Mario
Gašić, Miroslav J.
Sladić, Dušan
Article (Accepted Version)
Metadata
Show full item record
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.
Source:
Bioconjugate Chemistry, 2012, 23, 1, 57-65
Publisher:
  • American Chemical Society (ACS)
Funding / projects:
  • Interactions of natural products, their derivatives and coordination compounds with proteins and nucleic acids (RS-172055)
  • Deutscher Akademischer Austausch Dienst (DAAD)
Note:
  • This is the peer-reviewed version of the article: Novaković, I., Anđelković, U., Zlatović, M., Gašić, M.J., Sladić, D., 2012. Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives. Bioconjugate Chem. 23, 57–65. https://doi.org/10.1021/bc200330m

DOI: 10.1021/bc200330m

ISSN: 1043-1802

PubMed: 22148500

WoS: 000299591000007

Scopus: 2-s2.0-84855919661
[ Google Scholar ]
9
10
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/1005
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - JOUR
AU  - Novaković, Irena
AU  - Anđelković, Uroš
AU  - Zlatović, Mario
AU  - Gašić, Miroslav J.
AU  - Sladić, Dušan
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1005
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  - American Chemical Society (ACS)
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 and Anđelković, Uroš and Zlatović, Mario and Gašić, 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 = "American Chemical Society (ACS)",
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., Anđelković, U., Zlatović, M., Gašić, M. J.,& Sladić, D.. (2012). Bioconjugate of Lysozyme and the Antibacterial Marine Sesquiterpene Quinone Avarone and Its Derivatives. in Bioconjugate Chemistry
American Chemical Society (ACS)., 23(1), 57-65.
https://doi.org/10.1021/bc200330m
Novaković I, Anđelković U, Zlatović M, Gašić 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, Anđelković, Uroš, Zlatović, Mario, Gašić, 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 . .

DSpace software copyright © 2002-2015  DuraSpace
About CeR – Central Repository | Send Feedback

re3dataOpenAIRERCUB
 

 

All of DSpaceInstitutions/communitiesAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About CeR – Central Repository | Send Feedback

re3dataOpenAIRERCUB