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Human serum albumin binding of certain antimalarials

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Authors
Marković, Olivera S.
Cvijetić, Ilija
Zlatović, Mario V.
Opsenica, Igor
Terzić-Jovanović, Nataša V.
Šolaja, Bogdan A.
Verbić, Tatjana
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Abstract
Tested compounds, previously synthesized, are derivatives of chloroquine, drug commonly used in the treatment and prevention of malaria. Human serum albumin (HSA) has the role in transport of endogenous (fatty acids, hormones, bile acids, amino acids) and exogenous compounds (drug molecules and nutrients). Interaction between tested compounds and HSA has been studied by fluorescence spectroscopy in phosphate buffered saline (1× PBS, pH 7.4) [1]. Results show that among tested compounds, all positively charged at pH 7.4, derivatives with thiophene substructure bind to HSA. Molecular docking studies were used to determine HSA–compound binding mode. Fluorescence quenching data were processed using Stern-Volmer (S-V) equation [2]. Almost linear S-V plot for binding of 1 to HSA (Fig. 1a) indicates single type of quenching mechanism. Results show that Ksv decreases (20C: (2.60±0.07)×105 M -1 ; 25C: (2.33±0.07)×105 M -1 and 37C: (2.18±0.08)×105 M -1 ) as temperatu...re increases indicating static quenching mechanism. Downward curvature in S-V plots of 2 and 3 (Fig. 1b and 1c) indicates that tryptophan residues are not fully accessible to the drug and that dynamic quenching dominates over static. Fraction of tryptophan residues that are buried and inaccessible to the quencher and effective quenching constants can be determined by modified S-V equation. The effective quenching constant for 2 and 3 increases as temperature increases, this is another indication that dynamic quenching process is dominant in binding of 2 and 3 to HSA. Effective quenching constants of all three compounds are in the order of 10 5 M-1, meaning that these compounds can be effectively carried and stored by HSA in the human body.

Source:
4th World Conference on Physico-Chemical Methods in Drug Discovery and Development, Red Island, Croatia, September 21-24, 2015, 2015, 67-67
Funding / projects:
  • The synthesis of aminoquinoline-based antimalarials and botulinum neurotoxin A inhibitors (RS-172008)
  • 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-256716)
[ Google Scholar ]
Handle
https://hdl.handle.net/21.15107/rcub_cherry_5323
URI
http://cherry.chem.bg.ac.rs/handle/123456789/5323
Collections
  • Publikacije
Institution/Community
Hemijski fakultet
TY  - CONF
AU  - Marković, Olivera S.
AU  - Cvijetić, Ilija
AU  - Zlatović, Mario V.
AU  - Opsenica, Igor
AU  - Terzić-Jovanović, Nataša V.
AU  - Šolaja, Bogdan A.
AU  - Verbić, Tatjana
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5323
AB  - Tested compounds, previously synthesized, are derivatives of chloroquine, drug commonly 
used in the treatment and prevention of malaria. Human serum albumin (HSA) has the role in 
transport of endogenous (fatty acids, hormones, bile acids, amino acids) and exogenous 
compounds (drug molecules and nutrients). Interaction between tested compounds and HSA 
has been studied by fluorescence spectroscopy in phosphate buffered saline (1× PBS, pH 7.4) 
[1]. Results show that among tested compounds, all positively charged at pH 7.4, derivatives 
with thiophene substructure bind to HSA. Molecular docking studies were used to determine 
HSA–compound binding mode.
Fluorescence quenching data were processed using Stern-Volmer (S-V) equation [2]. Almost 
linear S-V plot for binding of 1 to HSA (Fig. 1a) indicates single type of quenching mechanism. 
Results show that Ksv decreases (20C: (2.60±0.07)×105 M
-1
; 25C: (2.33±0.07)×105 M
-1 and 
37C: (2.18±0.08)×105 M
-1
) as temperature increases indicating static quenching mechanism. 
Downward curvature in S-V plots of 2 and 3 (Fig. 1b and 1c) indicates that tryptophan residues 
are not fully accessible to the drug and that dynamic quenching dominates over static. Fraction 
of tryptophan residues that are buried and inaccessible to the quencher and effective 
quenching constants can be determined by modified S-V equation. The effective quenching 
constant for 2 and 3 increases as temperature increases, this is another indication that dynamic 
quenching process is dominant in binding of 2 and 3 to HSA. Effective quenching constants of 
all three compounds are in the order of 10 5 M-1, meaning that these compounds can be 
effectively carried and stored by HSA in the human body.
C3  - 4th World Conference on Physico-Chemical Methods in Drug Discovery and Development, Red Island, Croatia, September 21-24, 2015
T1  - Human serum albumin binding of certain antimalarials
SP  - 67
EP  - 67
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5323
ER  - 
@conference{
author = "Marković, Olivera S. and Cvijetić, Ilija and Zlatović, Mario V. and Opsenica, Igor and Terzić-Jovanović, Nataša V. and Šolaja, Bogdan A. and Verbić, Tatjana",
year = "2015",
abstract = "Tested compounds, previously synthesized, are derivatives of chloroquine, drug commonly 
used in the treatment and prevention of malaria. Human serum albumin (HSA) has the role in 
transport of endogenous (fatty acids, hormones, bile acids, amino acids) and exogenous 
compounds (drug molecules and nutrients). Interaction between tested compounds and HSA 
has been studied by fluorescence spectroscopy in phosphate buffered saline (1× PBS, pH 7.4) 
[1]. Results show that among tested compounds, all positively charged at pH 7.4, derivatives 
with thiophene substructure bind to HSA. Molecular docking studies were used to determine 
HSA–compound binding mode.
Fluorescence quenching data were processed using Stern-Volmer (S-V) equation [2]. Almost 
linear S-V plot for binding of 1 to HSA (Fig. 1a) indicates single type of quenching mechanism. 
Results show that Ksv decreases (20C: (2.60±0.07)×105 M
-1
; 25C: (2.33±0.07)×105 M
-1 and 
37C: (2.18±0.08)×105 M
-1
) as temperature increases indicating static quenching mechanism. 
Downward curvature in S-V plots of 2 and 3 (Fig. 1b and 1c) indicates that tryptophan residues 
are not fully accessible to the drug and that dynamic quenching dominates over static. Fraction 
of tryptophan residues that are buried and inaccessible to the quencher and effective 
quenching constants can be determined by modified S-V equation. The effective quenching 
constant for 2 and 3 increases as temperature increases, this is another indication that dynamic 
quenching process is dominant in binding of 2 and 3 to HSA. Effective quenching constants of 
all three compounds are in the order of 10 5 M-1, meaning that these compounds can be 
effectively carried and stored by HSA in the human body.",
journal = "4th World Conference on Physico-Chemical Methods in Drug Discovery and Development, Red Island, Croatia, September 21-24, 2015",
title = "Human serum albumin binding of certain antimalarials",
pages = "67-67",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5323"
}
Marković, O. S., Cvijetić, I., Zlatović, M. V., Opsenica, I., Terzić-Jovanović, N. V., Šolaja, B. A.,& Verbić, T.. (2015). Human serum albumin binding of certain antimalarials. in 4th World Conference on Physico-Chemical Methods in Drug Discovery and Development, Red Island, Croatia, September 21-24, 2015, 67-67.
https://hdl.handle.net/21.15107/rcub_cherry_5323
Marković OS, Cvijetić I, Zlatović MV, Opsenica I, Terzić-Jovanović NV, Šolaja BA, Verbić T. Human serum albumin binding of certain antimalarials. in 4th World Conference on Physico-Chemical Methods in Drug Discovery and Development, Red Island, Croatia, September 21-24, 2015. 2015;:67-67.
https://hdl.handle.net/21.15107/rcub_cherry_5323 .
Marković, Olivera S., Cvijetić, Ilija, Zlatović, Mario V., Opsenica, Igor, Terzić-Jovanović, Nataša V., Šolaja, Bogdan A., Verbić, Tatjana, "Human serum albumin binding of certain antimalarials" in 4th World Conference on Physico-Chemical Methods in Drug Discovery and Development, Red Island, Croatia, September 21-24, 2015 (2015):67-67,
https://hdl.handle.net/21.15107/rcub_cherry_5323 .

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