The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding
Само за регистроване кориснике
2019
Аутори
Penezić, Ana Z.Aćimović, Jelena M.
Pavićević, Ivan D.
Jovanović, Vesna B.
Takić, Marija
Mandić, Ljuba M.
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Cys34 thiol group of human serum albumin (HSA) represents major plasma antioxidant. Its reactivity is influenced by multiple factors. The influence of fatty acids (FA; saturated, mono, and poly unsaturated acids from fish oil) binding to HSA, on copper(II) binding affinity and Cys34 thiol group accessibility/reactivity, in the presence of carbonylation agent (methylglyoxal, MG) was examined. HSA-copper(II) content, thiol group reactivity, and HSA carbonylation level were monitored spectrophotometrically. Changes in HSA were followed by fluorescence spectroscopy and native PAG electrophoresis. FA/HSA molar ratio was screened by GC. Together, binding of copper(II) ions and FA to HSA increase the reactivity of Cys34 thiol group (depending on the type of FA), with constant contribution of copper(II) ions of one-third. Carbonylation of FA-HSA-Cu(II) complexes caused a decrease in the Cys34 thiol group content, accompanied by a decrease in the content of HSA-bound copper. The carbonylation l...evel of guanidine groups was not affected by FAs and copper(II) binding. Fluorescent emission spectra of FA-HSA-Cu(II)-MG complexes showed conformational changes in HSA molecule. Although binding of fatty acids and copper ions caused a significant increase in the thiol group reactivity, Cys34 thiol from FA-HSA-Cu(II) complexes reacted with MG in smaller extent than expected, probably as a consequence of conformational changes introduced by carbonylation. Increase in the percentage of reacted-free thiol groups with MG (due to FA and copper binding) may not seem to be very significant, but it is very important in complex biological systems, where catalytic metal is present. [GRAPHICS] .
Кључне речи:
Human serum albumin / Copper(II) / Fatty acids / Carbonylation / HSA Cys34 thiol group reactivityИзвор:
Journal of Biological Inorganic Chemistry, 2019, 24, 1, 61-70Издавач:
- Springer, New York
Финансирање / пројекти:
- Алергени, антитела, ензими и мали физиолошки значајни молекули: дизајн, структура, функција и значај (RS-MESTD-Basic Research (BR or ON)-172049)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-FP7-256716)
DOI: 10.1007/s00775-018-1628-7
ISSN: 0949-8257
PubMed: 30456476
WoS: 000459431600007
Scopus: 2-s2.0-85056852264
Институција/група
Institut za medicinska istraživanjaTY - JOUR AU - Penezić, Ana Z. AU - Aćimović, Jelena M. AU - Pavićević, Ivan D. AU - Jovanović, Vesna B. AU - Takić, Marija AU - Mandić, Ljuba M. PY - 2019 UR - http://rimi.imi.bg.ac.rs/handle/123456789/946 AB - Cys34 thiol group of human serum albumin (HSA) represents major plasma antioxidant. Its reactivity is influenced by multiple factors. The influence of fatty acids (FA; saturated, mono, and poly unsaturated acids from fish oil) binding to HSA, on copper(II) binding affinity and Cys34 thiol group accessibility/reactivity, in the presence of carbonylation agent (methylglyoxal, MG) was examined. HSA-copper(II) content, thiol group reactivity, and HSA carbonylation level were monitored spectrophotometrically. Changes in HSA were followed by fluorescence spectroscopy and native PAG electrophoresis. FA/HSA molar ratio was screened by GC. Together, binding of copper(II) ions and FA to HSA increase the reactivity of Cys34 thiol group (depending on the type of FA), with constant contribution of copper(II) ions of one-third. Carbonylation of FA-HSA-Cu(II) complexes caused a decrease in the Cys34 thiol group content, accompanied by a decrease in the content of HSA-bound copper. The carbonylation level of guanidine groups was not affected by FAs and copper(II) binding. Fluorescent emission spectra of FA-HSA-Cu(II)-MG complexes showed conformational changes in HSA molecule. Although binding of fatty acids and copper ions caused a significant increase in the thiol group reactivity, Cys34 thiol from FA-HSA-Cu(II) complexes reacted with MG in smaller extent than expected, probably as a consequence of conformational changes introduced by carbonylation. Increase in the percentage of reacted-free thiol groups with MG (due to FA and copper binding) may not seem to be very significant, but it is very important in complex biological systems, where catalytic metal is present. [GRAPHICS] . PB - Springer, New York T2 - Journal of Biological Inorganic Chemistry T1 - The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding EP - 70 IS - 1 SP - 61 VL - 24 DO - 10.1007/s00775-018-1628-7 ER -
@article{ author = "Penezić, Ana Z. and Aćimović, Jelena M. and Pavićević, Ivan D. and Jovanović, Vesna B. and Takić, Marija and Mandić, Ljuba M.", year = "2019", abstract = "Cys34 thiol group of human serum albumin (HSA) represents major plasma antioxidant. Its reactivity is influenced by multiple factors. The influence of fatty acids (FA; saturated, mono, and poly unsaturated acids from fish oil) binding to HSA, on copper(II) binding affinity and Cys34 thiol group accessibility/reactivity, in the presence of carbonylation agent (methylglyoxal, MG) was examined. HSA-copper(II) content, thiol group reactivity, and HSA carbonylation level were monitored spectrophotometrically. Changes in HSA were followed by fluorescence spectroscopy and native PAG electrophoresis. FA/HSA molar ratio was screened by GC. Together, binding of copper(II) ions and FA to HSA increase the reactivity of Cys34 thiol group (depending on the type of FA), with constant contribution of copper(II) ions of one-third. Carbonylation of FA-HSA-Cu(II) complexes caused a decrease in the Cys34 thiol group content, accompanied by a decrease in the content of HSA-bound copper. The carbonylation level of guanidine groups was not affected by FAs and copper(II) binding. Fluorescent emission spectra of FA-HSA-Cu(II)-MG complexes showed conformational changes in HSA molecule. Although binding of fatty acids and copper ions caused a significant increase in the thiol group reactivity, Cys34 thiol from FA-HSA-Cu(II) complexes reacted with MG in smaller extent than expected, probably as a consequence of conformational changes introduced by carbonylation. Increase in the percentage of reacted-free thiol groups with MG (due to FA and copper binding) may not seem to be very significant, but it is very important in complex biological systems, where catalytic metal is present. [GRAPHICS] .", publisher = "Springer, New York", journal = "Journal of Biological Inorganic Chemistry", title = "The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding", pages = "70-61", number = "1", volume = "24", doi = "10.1007/s00775-018-1628-7" }
Penezić, A. Z., Aćimović, J. M., Pavićević, I. D., Jovanović, V. B., Takić, M.,& Mandić, L. M.. (2019). The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding. in Journal of Biological Inorganic Chemistry Springer, New York., 24(1), 61-70. https://doi.org/10.1007/s00775-018-1628-7
Penezić AZ, Aćimović JM, Pavićević ID, Jovanović VB, Takić M, Mandić LM. The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding. in Journal of Biological Inorganic Chemistry. 2019;24(1):61-70. doi:10.1007/s00775-018-1628-7 .
Penezić, Ana Z., Aćimović, Jelena M., Pavićević, Ivan D., Jovanović, Vesna B., Takić, Marija, Mandić, Ljuba M., "The interplay between copper(II), human serum albumin, fatty acids, and carbonylating agent interferes with Cys 34 thiol reactivity and copper binding" in Journal of Biological Inorganic Chemistry, 24, no. 1 (2019):61-70, https://doi.org/10.1007/s00775-018-1628-7 . .