Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods

Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of t...
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Autor*in:	Ciuciu, Ana-Maria Simion [verfasserIn] Aprodu, Iuliana [verfasserIn] Alexe, Petru [verfasserIn] Stănciuc, Nicoleta [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2016

Schlagwörter:	β-lactoglobulin Retinol Thermodynamic parameters Fluorescence spectroscopy

Übergeordnetes Werk:	Enthalten in: Dairy science & technology - Berlin : Springer, 2008, 96(2016), 3 vom: 11. Jan., Seite 405-423
Übergeordnetes Werk:	volume:96 ; year:2016 ; number:3 ; day:11 ; month:01 ; pages:405-423

Links:	Volltext

DOI / URN:	10.1007/s13594-015-0277-7

Katalog-ID:	SPR03189223X

Internformat


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245	1	0	\|a Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods
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520			\|a Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities.
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650		4	\|a Thermodynamic parameters \|7 (dpeaa)DE-He213
650		4	\|a Fluorescence spectroscopy \|7 (dpeaa)DE-He213
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912			\|a GBV_ILN_230
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
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912			\|a GBV_ILN_2064
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912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2188
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
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912			\|a GBV_ILN_4126
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912			\|a GBV_ILN_4328
912			\|a GBV_ILN_4333
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912			\|a GBV_ILN_4367
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Indexfelder

author_variant	a m s c ams amsc i a ia p a pa n s ns
matchkey_str	article:19585594:2016----::hraldieitrcinbtenatgouiadeioaeaenetgtdyloecnepcr
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publishDate	2016
allfields	10.1007/s13594-015-0277-7 doi (DE-627)SPR03189223X (SPR)s13594-015-0277-7-e DE-627 ger DE-627 rakwb eng 630 640 ASE Ciuciu, Ana-Maria Simion verfasserin aut Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities. β-lactoglobulin (dpeaa)DE-He213 Retinol (dpeaa)DE-He213 Thermodynamic parameters (dpeaa)DE-He213 Fluorescence spectroscopy (dpeaa)DE-He213 Aprodu, Iuliana verfasserin aut Alexe, Petru verfasserin aut Stănciuc, Nicoleta verfasserin aut Enthalten in Dairy science & technology Berlin : Springer, 2008 96(2016), 3 vom: 11. Jan., Seite 405-423 (DE-627)633751677 (DE-600)2568727-X 1958-5594 nnns volume:96 year:2016 number:3 day:11 month:01 pages:405-423 https://dx.doi.org/10.1007/s13594-015-0277-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 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_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 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_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 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_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 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_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 96 2016 3 11 01 405-423
spelling	10.1007/s13594-015-0277-7 doi (DE-627)SPR03189223X (SPR)s13594-015-0277-7-e DE-627 ger DE-627 rakwb eng 630 640 ASE Ciuciu, Ana-Maria Simion verfasserin aut Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities. β-lactoglobulin (dpeaa)DE-He213 Retinol (dpeaa)DE-He213 Thermodynamic parameters (dpeaa)DE-He213 Fluorescence spectroscopy (dpeaa)DE-He213 Aprodu, Iuliana verfasserin aut Alexe, Petru verfasserin aut Stănciuc, Nicoleta verfasserin aut Enthalten in Dairy science & technology Berlin : Springer, 2008 96(2016), 3 vom: 11. Jan., Seite 405-423 (DE-627)633751677 (DE-600)2568727-X 1958-5594 nnns volume:96 year:2016 number:3 day:11 month:01 pages:405-423 https://dx.doi.org/10.1007/s13594-015-0277-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 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_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 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_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 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_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 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_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 96 2016 3 11 01 405-423
allfields_unstemmed	10.1007/s13594-015-0277-7 doi (DE-627)SPR03189223X (SPR)s13594-015-0277-7-e DE-627 ger DE-627 rakwb eng 630 640 ASE Ciuciu, Ana-Maria Simion verfasserin aut Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities. β-lactoglobulin (dpeaa)DE-He213 Retinol (dpeaa)DE-He213 Thermodynamic parameters (dpeaa)DE-He213 Fluorescence spectroscopy (dpeaa)DE-He213 Aprodu, Iuliana verfasserin aut Alexe, Petru verfasserin aut Stănciuc, Nicoleta verfasserin aut Enthalten in Dairy science & technology Berlin : Springer, 2008 96(2016), 3 vom: 11. Jan., Seite 405-423 (DE-627)633751677 (DE-600)2568727-X 1958-5594 nnns volume:96 year:2016 number:3 day:11 month:01 pages:405-423 https://dx.doi.org/10.1007/s13594-015-0277-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 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_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 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_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 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_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 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_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 96 2016 3 11 01 405-423
allfieldsGer	10.1007/s13594-015-0277-7 doi (DE-627)SPR03189223X (SPR)s13594-015-0277-7-e DE-627 ger DE-627 rakwb eng 630 640 ASE Ciuciu, Ana-Maria Simion verfasserin aut Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities. β-lactoglobulin (dpeaa)DE-He213 Retinol (dpeaa)DE-He213 Thermodynamic parameters (dpeaa)DE-He213 Fluorescence spectroscopy (dpeaa)DE-He213 Aprodu, Iuliana verfasserin aut Alexe, Petru verfasserin aut Stănciuc, Nicoleta verfasserin aut Enthalten in Dairy science & technology Berlin : Springer, 2008 96(2016), 3 vom: 11. Jan., Seite 405-423 (DE-627)633751677 (DE-600)2568727-X 1958-5594 nnns volume:96 year:2016 number:3 day:11 month:01 pages:405-423 https://dx.doi.org/10.1007/s13594-015-0277-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 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_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 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_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 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_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 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_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 96 2016 3 11 01 405-423
allfieldsSound	10.1007/s13594-015-0277-7 doi (DE-627)SPR03189223X (SPR)s13594-015-0277-7-e DE-627 ger DE-627 rakwb eng 630 640 ASE Ciuciu, Ana-Maria Simion verfasserin aut Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities. β-lactoglobulin (dpeaa)DE-He213 Retinol (dpeaa)DE-He213 Thermodynamic parameters (dpeaa)DE-He213 Fluorescence spectroscopy (dpeaa)DE-He213 Aprodu, Iuliana verfasserin aut Alexe, Petru verfasserin aut Stănciuc, Nicoleta verfasserin aut Enthalten in Dairy science & technology Berlin : Springer, 2008 96(2016), 3 vom: 11. Jan., Seite 405-423 (DE-627)633751677 (DE-600)2568727-X 1958-5594 nnns volume:96 year:2016 number:3 day:11 month:01 pages:405-423 https://dx.doi.org/10.1007/s13594-015-0277-7 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 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_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 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_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2106 GBV_ILN_2108 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_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 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_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 96 2016 3 11 01 405-423
language	English
source	Enthalten in Dairy science & technology 96(2016), 3 vom: 11. Jan., Seite 405-423 volume:96 year:2016 number:3 day:11 month:01 pages:405-423
sourceStr	Enthalten in Dairy science & technology 96(2016), 3 vom: 11. Jan., Seite 405-423 volume:96 year:2016 number:3 day:11 month:01 pages:405-423
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	β-lactoglobulin Retinol Thermodynamic parameters Fluorescence spectroscopy
dewey-raw	630
isfreeaccess_bool	false
container_title	Dairy science & technology
authorswithroles_txt_mv	Ciuciu, Ana-Maria Simion @@aut@@ Aprodu, Iuliana @@aut@@ Alexe, Petru @@aut@@ Stănciuc, Nicoleta @@aut@@
publishDateDaySort_date	2016-01-11T00:00:00Z
hierarchy_top_id	633751677
dewey-sort	3630
id	SPR03189223X
language_de	englisch
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author	Ciuciu, Ana-Maria Simion
spellingShingle	Ciuciu, Ana-Maria Simion ddc 630 misc β-lactoglobulin misc Retinol misc Thermodynamic parameters misc Fluorescence spectroscopy Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods
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topic_title	630 640 ASE Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods β-lactoglobulin (dpeaa)DE-He213 Retinol (dpeaa)DE-He213 Thermodynamic parameters (dpeaa)DE-He213 Fluorescence spectroscopy (dpeaa)DE-He213
topic	ddc 630 misc β-lactoglobulin misc Retinol misc Thermodynamic parameters misc Fluorescence spectroscopy
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title	Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods
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title_full	Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods
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author_browse	Ciuciu, Ana-Maria Simion Aprodu, Iuliana Alexe, Petru Stănciuc, Nicoleta
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title_sort	thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods
title_auth	Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods
abstract	Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities.
abstractGer	Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities.
abstract_unstemmed	Abstract Whey proteins have important functional properties as it can bind a wide range of bioactive molecules. In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. This study offers useful information on the potential use of βLG as a carrier for biologically active compounds in order to obtain food products with desired functionalities.
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title_short	Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods
url	https://dx.doi.org/10.1007/s13594-015-0277-7
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In this study, the complexation of β-lactoglobulin with retinol at alkaline pH was investigated. The fluorescence spectroscopy was used to determine the temperature dependent behavior of the β-lactoglobulin-retinol acetate (βLG-RET) ensemble. The pattern of protein unfolding in the temperature range of 25–85 °C was followed mainly considering the exposure of tryptophan (Trp) residues. The βLG-RET complex appeared rather stable in the 25–60 °C range, while further increase of the temperature caused partial unfolding. The anisotropy measurements indicated a more flexible conformation at temperature increase up to 80 °C. In addition, the in silico approach was used to complement the experimental results. Important changes in the interaction surface were observed after performing molecular dynamics simulations. The temperature increase caused important rearrangements of the amino acids of the EF loop involved in the interaction with the retinol molecule, which got twisted. These atomic level events induced a significant increase of the affinity between βLG and retinol. 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Thermally driven interactions between β-lactoglobulin and retinol acetate investigated by fluorescence spectroscopy and molecular modeling methods

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