Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin
2015
Аутори
Minić, SimeonMilčić, Miloš
Stanić-Vučinić, Dragana
Radibratović, Milica
Sotiroudis, Theodore G.
Nikolić, Milan
Ćirković Veličković, Tanja
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Human serum albumin (HSA) is an important regulator of the pharmacokinetic properties of bioactive compounds. Phycocyanobilin is a blue tetrapyrrole chromophore of C-phycocyanin with proven health-promoting activities. Despite its structural similarity to bilirubin, the conformation it adopts in aqueous solution is different and the pigment is more soluble than bilirubin. The aim of our study was to examine binding of phycocyanobilin for HSA and to investigate its competition with bilirubin. Based on a computational approach, we demonstrated two putative high-affinity binding pockets on HSA of virtually identical energies for the neutral and anion forms of bilirubin, but with slightly favorable predictions for anion forms of phycocyanobilin. Computational prediction of phycocyanobilin pK(a) values suggested a monoanion form to be the most stable form at physiological conditions. The computationally predicted binding sites for phycocyanobilin were identical to the two previously identif...ied binding sites for bilirubin (subdomains IB and IIA). Results obtained by protein and pigment fluorescence measurements, circular dichroism, and competition experiments confirmed high affinity (binding constant of 2.2 x 10(6) M-1 at 25 degrees C), stereo-selective binding of phycocyanobilin M-conformer to HSA and its competition with bilirubin, warfarin and hemin. Our experimental data confirm that phycocyanobilin binds to IB and IIA binding site of HSA with an affinity similar to bilirubin. In conditions characterized by an increased bilirubin plasma concentration, or intake of drugs binding to IB or IIA binding site, pharmacokinetics of phycocyanobilin may also be changed.
Извор:
RSC Advances, 2015, 5, 76, 61787-61798Издавач:
- Royal Soc Chemistry, Cambridge
Финансирање / пројекти:
- Рационални дизајн и синтеза биолошки активних и координационих једињења и функционалних материјала, релевантних у (био)нанотехнологији (RS-172035)
- Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-172024)
- 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)
DOI: 10.1039/c5ra05534b
ISSN: 2046-2069
WoS: 000358353100036
Scopus: 2-s2.0-84937791375
Институција/група
IHTMTY - JOUR AU - Minić, Simeon AU - Milčić, Miloš AU - Stanić-Vučinić, Dragana AU - Radibratović, Milica AU - Sotiroudis, Theodore G. AU - Nikolić, Milan AU - Ćirković Veličković, Tanja PY - 2015 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1624 AB - Human serum albumin (HSA) is an important regulator of the pharmacokinetic properties of bioactive compounds. Phycocyanobilin is a blue tetrapyrrole chromophore of C-phycocyanin with proven health-promoting activities. Despite its structural similarity to bilirubin, the conformation it adopts in aqueous solution is different and the pigment is more soluble than bilirubin. The aim of our study was to examine binding of phycocyanobilin for HSA and to investigate its competition with bilirubin. Based on a computational approach, we demonstrated two putative high-affinity binding pockets on HSA of virtually identical energies for the neutral and anion forms of bilirubin, but with slightly favorable predictions for anion forms of phycocyanobilin. Computational prediction of phycocyanobilin pK(a) values suggested a monoanion form to be the most stable form at physiological conditions. The computationally predicted binding sites for phycocyanobilin were identical to the two previously identified binding sites for bilirubin (subdomains IB and IIA). Results obtained by protein and pigment fluorescence measurements, circular dichroism, and competition experiments confirmed high affinity (binding constant of 2.2 x 10(6) M-1 at 25 degrees C), stereo-selective binding of phycocyanobilin M-conformer to HSA and its competition with bilirubin, warfarin and hemin. Our experimental data confirm that phycocyanobilin binds to IB and IIA binding site of HSA with an affinity similar to bilirubin. In conditions characterized by an increased bilirubin plasma concentration, or intake of drugs binding to IB or IIA binding site, pharmacokinetics of phycocyanobilin may also be changed. PB - Royal Soc Chemistry, Cambridge T2 - RSC Advances T1 - Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin VL - 5 IS - 76 SP - 61787 EP - 61798 DO - 10.1039/c5ra05534b ER -
@article{ author = "Minić, Simeon and Milčić, Miloš and Stanić-Vučinić, Dragana and Radibratović, Milica and Sotiroudis, Theodore G. and Nikolić, Milan and Ćirković Veličković, Tanja", year = "2015", abstract = "Human serum albumin (HSA) is an important regulator of the pharmacokinetic properties of bioactive compounds. Phycocyanobilin is a blue tetrapyrrole chromophore of C-phycocyanin with proven health-promoting activities. Despite its structural similarity to bilirubin, the conformation it adopts in aqueous solution is different and the pigment is more soluble than bilirubin. The aim of our study was to examine binding of phycocyanobilin for HSA and to investigate its competition with bilirubin. Based on a computational approach, we demonstrated two putative high-affinity binding pockets on HSA of virtually identical energies for the neutral and anion forms of bilirubin, but with slightly favorable predictions for anion forms of phycocyanobilin. Computational prediction of phycocyanobilin pK(a) values suggested a monoanion form to be the most stable form at physiological conditions. The computationally predicted binding sites for phycocyanobilin were identical to the two previously identified binding sites for bilirubin (subdomains IB and IIA). Results obtained by protein and pigment fluorescence measurements, circular dichroism, and competition experiments confirmed high affinity (binding constant of 2.2 x 10(6) M-1 at 25 degrees C), stereo-selective binding of phycocyanobilin M-conformer to HSA and its competition with bilirubin, warfarin and hemin. Our experimental data confirm that phycocyanobilin binds to IB and IIA binding site of HSA with an affinity similar to bilirubin. In conditions characterized by an increased bilirubin plasma concentration, or intake of drugs binding to IB or IIA binding site, pharmacokinetics of phycocyanobilin may also be changed.", publisher = "Royal Soc Chemistry, Cambridge", journal = "RSC Advances", title = "Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin", volume = "5", number = "76", pages = "61787-61798", doi = "10.1039/c5ra05534b" }
Minić, S., Milčić, M., Stanić-Vučinić, D., Radibratović, M., Sotiroudis, T. G., Nikolić, M.,& Ćirković Veličković, T.. (2015). Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin. in RSC Advances Royal Soc Chemistry, Cambridge., 5(76), 61787-61798. https://doi.org/10.1039/c5ra05534b
Minić S, Milčić M, Stanić-Vučinić D, Radibratović M, Sotiroudis TG, Nikolić M, Ćirković Veličković T. Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin. in RSC Advances. 2015;5(76):61787-61798. doi:10.1039/c5ra05534b .
Minić, Simeon, Milčić, Miloš, Stanić-Vučinić, Dragana, Radibratović, Milica, Sotiroudis, Theodore G., Nikolić, Milan, Ćirković Veličković, Tanja, "Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin" in RSC Advances, 5, no. 76 (2015):61787-61798, https://doi.org/10.1039/c5ra05534b . .