Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters
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Interactions of 2-[(carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic acid (compound 1) and its mono-Me ester (compound 2) with the human serum albumin (HSA) have been studied by fluorescence spectroscopy. Comp. 1 exerts antiproliferative activity toward human tumor cells and significant selectivity (tumor vs. healthy cells) in vitro. Competitive binding study with warfarin and ibuprofen as binding site probes, revealed that one molecule of comp. 1 selectively binds to HSA Sudlow site I (warfarin site) with moderate binding constant (Kb = (2.8 ± 0.5) × 104 M-1 at 37 ± 1 °C), while comp. 2 binds to Sudlow site II (Kb = (3.2 ± 0.9) × 104 M-1 at 37 ± 1 °C). Fluorescence quenching at different temperatures was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. Energy resonance transfer between HSA and comp. 1 was examined according to Förster's non-radiative energy transfer theory. Distance of about 10 Å between ligand and Trp214 (HSA)... was obtained. Docking studies confirmed HSA Sudlow site I as a preferable comp. 1 binding site, and Sudlow site II as comp. 2 binding site. Molecular dynamics simulations proved the stability of comp. 1/HSA complex. © 2014 by the authors.
Кључне речи:
Competitive binding / Fluorescence spectroscopy / Molecular docking / Molecular dynamicsИзвор:
ADMET and DMPK, 2014, 2, 2, 126-142Финансирање / пројекти:
- High-Performance Computing Infrastructure for South East Europe's Research Communities (EU-261499)
- Рационални дизајн и синтеза биолошки активних и координационих једињења и функционалних материјала, релевантних у (био)нанотехнологији (RS-172035)
- 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)
Институција/група
IHTMTY - JOUR AU - Cvijetić, Ilija AU - Petrović, D.D. AU - Verbić, Tatjana AU - Juranić, Ivan AU - Drakulić, Branko PY - 2014 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/2669 AB - Interactions of 2-[(carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic acid (compound 1) and its mono-Me ester (compound 2) with the human serum albumin (HSA) have been studied by fluorescence spectroscopy. Comp. 1 exerts antiproliferative activity toward human tumor cells and significant selectivity (tumor vs. healthy cells) in vitro. Competitive binding study with warfarin and ibuprofen as binding site probes, revealed that one molecule of comp. 1 selectively binds to HSA Sudlow site I (warfarin site) with moderate binding constant (Kb = (2.8 ± 0.5) × 104 M-1 at 37 ± 1 °C), while comp. 2 binds to Sudlow site II (Kb = (3.2 ± 0.9) × 104 M-1 at 37 ± 1 °C). Fluorescence quenching at different temperatures was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. Energy resonance transfer between HSA and comp. 1 was examined according to Förster's non-radiative energy transfer theory. Distance of about 10 Å between ligand and Trp214 (HSA) was obtained. Docking studies confirmed HSA Sudlow site I as a preferable comp. 1 binding site, and Sudlow site II as comp. 2 binding site. Molecular dynamics simulations proved the stability of comp. 1/HSA complex. © 2014 by the authors. T2 - ADMET and DMPK T1 - Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters VL - 2 IS - 2 SP - 126 EP - 142 DO - 10.5599/admet.2.2.28 ER -
@article{ author = "Cvijetić, Ilija and Petrović, D.D. and Verbić, Tatjana and Juranić, Ivan and Drakulić, Branko", year = "2014", abstract = "Interactions of 2-[(carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic acid (compound 1) and its mono-Me ester (compound 2) with the human serum albumin (HSA) have been studied by fluorescence spectroscopy. Comp. 1 exerts antiproliferative activity toward human tumor cells and significant selectivity (tumor vs. healthy cells) in vitro. Competitive binding study with warfarin and ibuprofen as binding site probes, revealed that one molecule of comp. 1 selectively binds to HSA Sudlow site I (warfarin site) with moderate binding constant (Kb = (2.8 ± 0.5) × 104 M-1 at 37 ± 1 °C), while comp. 2 binds to Sudlow site II (Kb = (3.2 ± 0.9) × 104 M-1 at 37 ± 1 °C). Fluorescence quenching at different temperatures was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. Energy resonance transfer between HSA and comp. 1 was examined according to Förster's non-radiative energy transfer theory. Distance of about 10 Å between ligand and Trp214 (HSA) was obtained. Docking studies confirmed HSA Sudlow site I as a preferable comp. 1 binding site, and Sudlow site II as comp. 2 binding site. Molecular dynamics simulations proved the stability of comp. 1/HSA complex. © 2014 by the authors.", journal = "ADMET and DMPK", title = "Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters", volume = "2", number = "2", pages = "126-142", doi = "10.5599/admet.2.2.28" }
Cvijetić, I., Petrović, D.D., Verbić, T., Juranić, I.,& Drakulić, B.. (2014). Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters. in ADMET and DMPK, 2(2), 126-142. https://doi.org/10.5599/admet.2.2.28
Cvijetić I, Petrović D, Verbić T, Juranić I, Drakulić B. Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters. in ADMET and DMPK. 2014;2(2):126-142. doi:10.5599/admet.2.2.28 .
Cvijetić, Ilija, Petrović, D.D., Verbić, Tatjana, Juranić, Ivan, Drakulić, Branko, "Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters" in ADMET and DMPK, 2, no. 2 (2014):126-142, https://doi.org/10.5599/admet.2.2.28 . .