Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution
Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modelin...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Tang, Jiang-Hong [verfasserIn] Liang, Guo-Bin [verfasserIn] Zheng, Chun-Zhi [verfasserIn] Lian, Ning [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2012 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Journal of solution chemistry - New York, NY [u.a.] : Springer Science + Business Media B.V., 1972, 42(2012), 1 vom: 08. Dez., Seite 226-238 |
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| Übergeordnetes Werk: |
volume:42 ; year:2012 ; number:1 ; day:08 ; month:12 ; pages:226-238 |
| Links: |
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| DOI / URN: |
10.1007/s10953-012-9938-9 |
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| Katalog-ID: |
SPR01498654X |
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| 520 | |a Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. | ||
| 650 | 4 | |a Ellagic acid |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Human serum albumin |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Binding |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Aqueous solution |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Liang, Guo-Bin |e verfasserin |4 aut | |
| 700 | 1 | |a Zheng, Chun-Zhi |e verfasserin |4 aut | |
| 700 | 1 | |a Lian, Ning |e verfasserin |4 aut | |
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10.1007/s10953-012-9938-9 doi (DE-627)SPR01498654X (SPR)s10953-012-9938-9-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Tang, Jiang-Hong verfasserin aut Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. Ellagic acid (dpeaa)DE-He213 Human serum albumin (dpeaa)DE-He213 Binding (dpeaa)DE-He213 Aqueous solution (dpeaa)DE-He213 Liang, Guo-Bin verfasserin aut Zheng, Chun-Zhi verfasserin aut Lian, Ning verfasserin aut Enthalten in Journal of solution chemistry New York, NY [u.a.] : Springer Science + Business Media B.V., 1972 42(2012), 1 vom: 08. Dez., Seite 226-238 (DE-627)317881876 (DE-600)2017287-4 1572-8927 nnns volume:42 year:2012 number:1 day:08 month:12 pages:226-238 https://dx.doi.org/10.1007/s10953-012-9938-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 42 2012 1 08 12 226-238 |
| spelling |
10.1007/s10953-012-9938-9 doi (DE-627)SPR01498654X (SPR)s10953-012-9938-9-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Tang, Jiang-Hong verfasserin aut Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. Ellagic acid (dpeaa)DE-He213 Human serum albumin (dpeaa)DE-He213 Binding (dpeaa)DE-He213 Aqueous solution (dpeaa)DE-He213 Liang, Guo-Bin verfasserin aut Zheng, Chun-Zhi verfasserin aut Lian, Ning verfasserin aut Enthalten in Journal of solution chemistry New York, NY [u.a.] : Springer Science + Business Media B.V., 1972 42(2012), 1 vom: 08. Dez., Seite 226-238 (DE-627)317881876 (DE-600)2017287-4 1572-8927 nnns volume:42 year:2012 number:1 day:08 month:12 pages:226-238 https://dx.doi.org/10.1007/s10953-012-9938-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 42 2012 1 08 12 226-238 |
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10.1007/s10953-012-9938-9 doi (DE-627)SPR01498654X (SPR)s10953-012-9938-9-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Tang, Jiang-Hong verfasserin aut Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. Ellagic acid (dpeaa)DE-He213 Human serum albumin (dpeaa)DE-He213 Binding (dpeaa)DE-He213 Aqueous solution (dpeaa)DE-He213 Liang, Guo-Bin verfasserin aut Zheng, Chun-Zhi verfasserin aut Lian, Ning verfasserin aut Enthalten in Journal of solution chemistry New York, NY [u.a.] : Springer Science + Business Media B.V., 1972 42(2012), 1 vom: 08. Dez., Seite 226-238 (DE-627)317881876 (DE-600)2017287-4 1572-8927 nnns volume:42 year:2012 number:1 day:08 month:12 pages:226-238 https://dx.doi.org/10.1007/s10953-012-9938-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 42 2012 1 08 12 226-238 |
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10.1007/s10953-012-9938-9 doi (DE-627)SPR01498654X (SPR)s10953-012-9938-9-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Tang, Jiang-Hong verfasserin aut Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. Ellagic acid (dpeaa)DE-He213 Human serum albumin (dpeaa)DE-He213 Binding (dpeaa)DE-He213 Aqueous solution (dpeaa)DE-He213 Liang, Guo-Bin verfasserin aut Zheng, Chun-Zhi verfasserin aut Lian, Ning verfasserin aut Enthalten in Journal of solution chemistry New York, NY [u.a.] : Springer Science + Business Media B.V., 1972 42(2012), 1 vom: 08. Dez., Seite 226-238 (DE-627)317881876 (DE-600)2017287-4 1572-8927 nnns volume:42 year:2012 number:1 day:08 month:12 pages:226-238 https://dx.doi.org/10.1007/s10953-012-9938-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 42 2012 1 08 12 226-238 |
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10.1007/s10953-012-9938-9 doi (DE-627)SPR01498654X (SPR)s10953-012-9938-9-e DE-627 ger DE-627 rakwb eng 540 ASE 35.00 bkl Tang, Jiang-Hong verfasserin aut Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. Ellagic acid (dpeaa)DE-He213 Human serum albumin (dpeaa)DE-He213 Binding (dpeaa)DE-He213 Aqueous solution (dpeaa)DE-He213 Liang, Guo-Bin verfasserin aut Zheng, Chun-Zhi verfasserin aut Lian, Ning verfasserin aut Enthalten in Journal of solution chemistry New York, NY [u.a.] : Springer Science + Business Media B.V., 1972 42(2012), 1 vom: 08. Dez., Seite 226-238 (DE-627)317881876 (DE-600)2017287-4 1572-8927 nnns volume:42 year:2012 number:1 day:08 month:12 pages:226-238 https://dx.doi.org/10.1007/s10953-012-9938-9 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE AR 42 2012 1 08 12 226-238 |
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Enthalten in Journal of solution chemistry 42(2012), 1 vom: 08. Dez., Seite 226-238 volume:42 year:2012 number:1 day:08 month:12 pages:226-238 |
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Ellagic acid Human serum albumin Binding Aqueous solution |
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Tang, Jiang-Hong @@aut@@ Liang, Guo-Bin @@aut@@ Zheng, Chun-Zhi @@aut@@ Lian, Ning @@aut@@ |
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To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. 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Tang, Jiang-Hong |
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Tang, Jiang-Hong ddc 540 bkl 35.00 misc Ellagic acid misc Human serum albumin misc Binding misc Aqueous solution Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution |
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540 ASE 35.00 bkl Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution Ellagic acid (dpeaa)DE-He213 Human serum albumin (dpeaa)DE-He213 Binding (dpeaa)DE-He213 Aqueous solution (dpeaa)DE-He213 |
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Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution |
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Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution |
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Tang, Jiang-Hong Liang, Guo-Bin Zheng, Chun-Zhi Lian, Ning |
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investigation on the binding behavior of ellagic acid to human serum albumin in aqueous solution |
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Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution |
| abstract |
Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. |
| abstractGer |
Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. |
| abstract_unstemmed |
Abstract Ellagic acid (EA), one of the polyphenols in fruits and nuts, has pharmacological activity. To explore binding behavior of EA to protein, human serum albumin (HSA) was chosen and investigated by fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy and molecular modeling in aqueous solution. Fluorescence titration results indicated that EA effectively quenched the intrinsic fluorescence of HSA by static quenching and the binding process was spontaneous. According to the Scatchard equation, there was only one class of binding sites can bind to HSA, the binding constants at three different temperatures (298, 310 and 318 K) were 8.47 × $ 10^{4} $, 7.39 × $ 10^{4} $ and 6.00 × $ 10^{4} $, respectively. It was found by FT-IR spectra that EA altered HSA secondary structure. Thermodynamic analysis showed that hydrophobic interaction and hydrogen bonds played an important role in stabilizing EA–HSA complex. A molecular docking study suggested that the HSA residues for EA binding located in sub-domain IIA. |
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| title_short |
Investigation on the Binding Behavior of Ellagic Acid to Human Serum Albumin in Aqueous Solution |
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https://dx.doi.org/10.1007/s10953-012-9938-9 |
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| author2 |
Liang, Guo-Bin Zheng, Chun-Zhi Lian, Ning |
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Liang, Guo-Bin Zheng, Chun-Zhi Lian, Ning |
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| doi_str |
10.1007/s10953-012-9938-9 |
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2024-07-04T03:42:01.835Z |
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| score |
7.4017916 |