The influence of the flavonoid quercetin on the interaction of propranolol with human serum albumin: Experimental and theoretical approaches
The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed tha...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Mohseni-Shahri, Fatemeh S. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014transfer abstract |
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| Schlagwörter: |
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| Umfang: |
12 |
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| Übergeordnetes Werk: |
Enthalten in: New ablation evolution behaviors in micro-hole drilling of 2.5D C - Liu, Chang ELSEVIER, 2021, New York, NY [u.a.] |
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| Übergeordnetes Werk: |
volume:154 ; year:2014 ; pages:229-240 ; extent:12 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.jlumin.2014.04.033 |
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ELV023179449 |
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| 245 | 1 | 4 | |a The influence of the flavonoid quercetin on the interaction of propranolol with human serum albumin: Experimental and theoretical approaches |
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| 520 | |a The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. | ||
| 520 | |a The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. | ||
| 650 | 7 | |a Binding constant |2 Elsevier | |
| 650 | 7 | |a Binding site |2 Elsevier | |
| 650 | 7 | |a Secondary structure |2 Elsevier | |
| 650 | 7 | |a Conformational change |2 Elsevier | |
| 650 | 7 | |a Fluorescence quenching |2 Elsevier | |
| 700 | 1 | |a Housaindokht, Mohammad R. |4 oth | |
| 700 | 1 | |a Bozorgmehr, Mohammad R. |4 oth | |
| 700 | 1 | |a Moosavi-Movahedi, Ali A. |4 oth | |
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10.1016/j.jlumin.2014.04.033 doi GBVA2014022000026.pica (DE-627)ELV023179449 (ELSEVIER)S0022-2313(14)00272-5 DE-627 ger DE-627 rakwb eng 530 530 DE-600 670 VZ 51.60 bkl 58.45 bkl Mohseni-Shahri, Fatemeh S. verfasserin aut The influence of the flavonoid quercetin on the interaction of propranolol with human serum albumin: Experimental and theoretical approaches 2014transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. Binding constant Elsevier Binding site Elsevier Secondary structure Elsevier Conformational change Elsevier Fluorescence quenching Elsevier Housaindokht, Mohammad R. oth Bozorgmehr, Mohammad R. oth Moosavi-Movahedi, Ali A. oth Enthalten in Elsevier Liu, Chang ELSEVIER New ablation evolution behaviors in micro-hole drilling of 2.5D C 2021 New York, NY [u.a.] (DE-627)ELV00662605X volume:154 year:2014 pages:229-240 extent:12 https://doi.org/10.1016/j.jlumin.2014.04.033 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 154 2014 229-240 12 045F 530 |
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10.1016/j.jlumin.2014.04.033 doi GBVA2014022000026.pica (DE-627)ELV023179449 (ELSEVIER)S0022-2313(14)00272-5 DE-627 ger DE-627 rakwb eng 530 530 DE-600 670 VZ 51.60 bkl 58.45 bkl Mohseni-Shahri, Fatemeh S. verfasserin aut The influence of the flavonoid quercetin on the interaction of propranolol with human serum albumin: Experimental and theoretical approaches 2014transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. Binding constant Elsevier Binding site Elsevier Secondary structure Elsevier Conformational change Elsevier Fluorescence quenching Elsevier Housaindokht, Mohammad R. oth Bozorgmehr, Mohammad R. oth Moosavi-Movahedi, Ali A. oth Enthalten in Elsevier Liu, Chang ELSEVIER New ablation evolution behaviors in micro-hole drilling of 2.5D C 2021 New York, NY [u.a.] (DE-627)ELV00662605X volume:154 year:2014 pages:229-240 extent:12 https://doi.org/10.1016/j.jlumin.2014.04.033 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 154 2014 229-240 12 045F 530 |
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10.1016/j.jlumin.2014.04.033 doi GBVA2014022000026.pica (DE-627)ELV023179449 (ELSEVIER)S0022-2313(14)00272-5 DE-627 ger DE-627 rakwb eng 530 530 DE-600 670 VZ 51.60 bkl 58.45 bkl Mohseni-Shahri, Fatemeh S. verfasserin aut The influence of the flavonoid quercetin on the interaction of propranolol with human serum albumin: Experimental and theoretical approaches 2014transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. Binding constant Elsevier Binding site Elsevier Secondary structure Elsevier Conformational change Elsevier Fluorescence quenching Elsevier Housaindokht, Mohammad R. oth Bozorgmehr, Mohammad R. oth Moosavi-Movahedi, Ali A. oth Enthalten in Elsevier Liu, Chang ELSEVIER New ablation evolution behaviors in micro-hole drilling of 2.5D C 2021 New York, NY [u.a.] (DE-627)ELV00662605X volume:154 year:2014 pages:229-240 extent:12 https://doi.org/10.1016/j.jlumin.2014.04.033 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 154 2014 229-240 12 045F 530 |
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10.1016/j.jlumin.2014.04.033 doi GBVA2014022000026.pica (DE-627)ELV023179449 (ELSEVIER)S0022-2313(14)00272-5 DE-627 ger DE-627 rakwb eng 530 530 DE-600 670 VZ 51.60 bkl 58.45 bkl Mohseni-Shahri, Fatemeh S. verfasserin aut The influence of the flavonoid quercetin on the interaction of propranolol with human serum albumin: Experimental and theoretical approaches 2014transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. Binding constant Elsevier Binding site Elsevier Secondary structure Elsevier Conformational change Elsevier Fluorescence quenching Elsevier Housaindokht, Mohammad R. oth Bozorgmehr, Mohammad R. oth Moosavi-Movahedi, Ali A. oth Enthalten in Elsevier Liu, Chang ELSEVIER New ablation evolution behaviors in micro-hole drilling of 2.5D C 2021 New York, NY [u.a.] (DE-627)ELV00662605X volume:154 year:2014 pages:229-240 extent:12 https://doi.org/10.1016/j.jlumin.2014.04.033 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 154 2014 229-240 12 045F 530 |
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10.1016/j.jlumin.2014.04.033 doi GBVA2014022000026.pica (DE-627)ELV023179449 (ELSEVIER)S0022-2313(14)00272-5 DE-627 ger DE-627 rakwb eng 530 530 DE-600 670 VZ 51.60 bkl 58.45 bkl Mohseni-Shahri, Fatemeh S. verfasserin aut The influence of the flavonoid quercetin on the interaction of propranolol with human serum albumin: Experimental and theoretical approaches 2014transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. Binding constant Elsevier Binding site Elsevier Secondary structure Elsevier Conformational change Elsevier Fluorescence quenching Elsevier Housaindokht, Mohammad R. oth Bozorgmehr, Mohammad R. oth Moosavi-Movahedi, Ali A. oth Enthalten in Elsevier Liu, Chang ELSEVIER New ablation evolution behaviors in micro-hole drilling of 2.5D C 2021 New York, NY [u.a.] (DE-627)ELV00662605X volume:154 year:2014 pages:229-240 extent:12 https://doi.org/10.1016/j.jlumin.2014.04.033 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 154 2014 229-240 12 045F 530 |
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The influence of the flavonoid quercetin on the interaction of propranolol with human serum albumin: Experimental and theoretical approaches |
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The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. |
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The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. |
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The binding of propranolol (PROP) to human serum albumin (HSA) in the absence and presence of quercetin (QUER) in aqueous solution was investigated by multiple techniques. The presence of quercetin (QUER) increased binding constant of propranolol (PROP) with HSA. Fluorescence spectroscopy showed that quercetin (QUER) could quench the HSA fluorescence spectra. The results of synchronous fluorescence, resonance light scattering (RLS) and three-dimensional fluorescence spectra showed that propranolol (PROP) and quercetin (QUER) would alter the micro-environment around tryptophan (Trp) and tyrosine (Tyr) residues. According molecular dynamics (MD) simulation results suggested that these ligands can interact with the protein, with affecting the secondary structure of HSA and with a modification of its tertiary structure. Molecular docking studies showed that the affinity and binding site of each of the ligands to HSA altered in the presence of the other. All above results may have related consequence in rationalizing the interferences of ordinary food to cardiac dysrhythmias treatments. |
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