4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor

β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind...
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Autor*in:	Xiao-Long Hu [verfasserIn] Ye-Bo Li [verfasserIn] Song Qi [verfasserIn] Qiao Zhang [verfasserIn] Tian-Shu Ren [verfasserIn] Wei-Hong Meng [verfasserIn] Qing-Chun Zhao [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2016

Schlagwörter:	Alzheimer's disease (AD) β-secretase (BACE1) β-amyloid peptide Paeonia lactiflora Pall 4-O-galloylalbiflorin Docking

Übergeordnetes Werk:	In: Journal of Functional Foods - Elsevier, 2021, 27(2016), Seite 517-525
Übergeordnetes Werk:	volume:27 ; year:2016 ; pages:517-525

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.jff.2016.10.012

Katalog-ID:	DOAJ073546100

Internformat


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520			\|a β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs.
650		4	\|a Alzheimer's disease (AD)
650		4	\|a β-secretase (BACE1)
650		4	\|a β-amyloid peptide
650		4	\|a Paeonia lactiflora Pall
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650		4	\|a Docking
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700	0		\|a Tian-Shu Ren \|e verfasserin \|4 aut
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700	0		\|a Qing-Chun Zhao \|e verfasserin \|4 aut
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912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_165
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
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912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2037
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2039
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912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
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912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2056
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2098
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2116
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2119
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2188
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
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912			\|a GBV_ILN_4037
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912			\|a GBV_ILN_4333
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912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4338
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author_variant	x l h xlh y b l ybl s q sq q z qz t s r tsr w h m whm q c z qcz
matchkey_str	article:22149414:2016----::oalyabfoidsoeefopenaatfoaalsptniliemlipeusrrt
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allfields	10.1016/j.jff.2016.10.012 doi (DE-627)DOAJ073546100 (DE-599)DOAJdca3d6c8541c45e5808fd66405f11332 DE-627 ger DE-627 rakwb eng TX341-641 Xiao-Long Hu verfasserin aut 4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs. Alzheimer's disease (AD) β-secretase (BACE1) β-amyloid peptide Paeonia lactiflora Pall 4-O-galloylalbiflorin Docking Nutrition. Foods and food supply Ye-Bo Li verfasserin aut Song Qi verfasserin aut Qiao Zhang verfasserin aut Tian-Shu Ren verfasserin aut Wei-Hong Meng verfasserin aut Qing-Chun Zhao verfasserin aut In Journal of Functional Foods Elsevier, 2021 27(2016), Seite 517-525 (DE-627)587138432 (DE-600)2467241-5 22149414 nnns volume:27 year:2016 pages:517-525 https://doi.org/10.1016/j.jff.2016.10.012 kostenfrei https://doaj.org/article/dca3d6c8541c45e5808fd66405f11332 kostenfrei http://www.sciencedirect.com/science/article/pii/S1756464616303255 kostenfrei https://doaj.org/toc/1756-4646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 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_2056 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_2098 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 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_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2016 517-525
spelling	10.1016/j.jff.2016.10.012 doi (DE-627)DOAJ073546100 (DE-599)DOAJdca3d6c8541c45e5808fd66405f11332 DE-627 ger DE-627 rakwb eng TX341-641 Xiao-Long Hu verfasserin aut 4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs. Alzheimer's disease (AD) β-secretase (BACE1) β-amyloid peptide Paeonia lactiflora Pall 4-O-galloylalbiflorin Docking Nutrition. Foods and food supply Ye-Bo Li verfasserin aut Song Qi verfasserin aut Qiao Zhang verfasserin aut Tian-Shu Ren verfasserin aut Wei-Hong Meng verfasserin aut Qing-Chun Zhao verfasserin aut In Journal of Functional Foods Elsevier, 2021 27(2016), Seite 517-525 (DE-627)587138432 (DE-600)2467241-5 22149414 nnns volume:27 year:2016 pages:517-525 https://doi.org/10.1016/j.jff.2016.10.012 kostenfrei https://doaj.org/article/dca3d6c8541c45e5808fd66405f11332 kostenfrei http://www.sciencedirect.com/science/article/pii/S1756464616303255 kostenfrei https://doaj.org/toc/1756-4646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 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_2056 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_2098 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 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_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2016 517-525
allfields_unstemmed	10.1016/j.jff.2016.10.012 doi (DE-627)DOAJ073546100 (DE-599)DOAJdca3d6c8541c45e5808fd66405f11332 DE-627 ger DE-627 rakwb eng TX341-641 Xiao-Long Hu verfasserin aut 4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs. Alzheimer's disease (AD) β-secretase (BACE1) β-amyloid peptide Paeonia lactiflora Pall 4-O-galloylalbiflorin Docking Nutrition. Foods and food supply Ye-Bo Li verfasserin aut Song Qi verfasserin aut Qiao Zhang verfasserin aut Tian-Shu Ren verfasserin aut Wei-Hong Meng verfasserin aut Qing-Chun Zhao verfasserin aut In Journal of Functional Foods Elsevier, 2021 27(2016), Seite 517-525 (DE-627)587138432 (DE-600)2467241-5 22149414 nnns volume:27 year:2016 pages:517-525 https://doi.org/10.1016/j.jff.2016.10.012 kostenfrei https://doaj.org/article/dca3d6c8541c45e5808fd66405f11332 kostenfrei http://www.sciencedirect.com/science/article/pii/S1756464616303255 kostenfrei https://doaj.org/toc/1756-4646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 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_2056 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_2098 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 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_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2016 517-525
allfieldsGer	10.1016/j.jff.2016.10.012 doi (DE-627)DOAJ073546100 (DE-599)DOAJdca3d6c8541c45e5808fd66405f11332 DE-627 ger DE-627 rakwb eng TX341-641 Xiao-Long Hu verfasserin aut 4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs. Alzheimer's disease (AD) β-secretase (BACE1) β-amyloid peptide Paeonia lactiflora Pall 4-O-galloylalbiflorin Docking Nutrition. Foods and food supply Ye-Bo Li verfasserin aut Song Qi verfasserin aut Qiao Zhang verfasserin aut Tian-Shu Ren verfasserin aut Wei-Hong Meng verfasserin aut Qing-Chun Zhao verfasserin aut In Journal of Functional Foods Elsevier, 2021 27(2016), Seite 517-525 (DE-627)587138432 (DE-600)2467241-5 22149414 nnns volume:27 year:2016 pages:517-525 https://doi.org/10.1016/j.jff.2016.10.012 kostenfrei https://doaj.org/article/dca3d6c8541c45e5808fd66405f11332 kostenfrei http://www.sciencedirect.com/science/article/pii/S1756464616303255 kostenfrei https://doaj.org/toc/1756-4646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 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_2056 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_2098 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 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_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2016 517-525
allfieldsSound	10.1016/j.jff.2016.10.012 doi (DE-627)DOAJ073546100 (DE-599)DOAJdca3d6c8541c45e5808fd66405f11332 DE-627 ger DE-627 rakwb eng TX341-641 Xiao-Long Hu verfasserin aut 4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor 2016 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs. Alzheimer's disease (AD) β-secretase (BACE1) β-amyloid peptide Paeonia lactiflora Pall 4-O-galloylalbiflorin Docking Nutrition. Foods and food supply Ye-Bo Li verfasserin aut Song Qi verfasserin aut Qiao Zhang verfasserin aut Tian-Shu Ren verfasserin aut Wei-Hong Meng verfasserin aut Qing-Chun Zhao verfasserin aut In Journal of Functional Foods Elsevier, 2021 27(2016), Seite 517-525 (DE-627)587138432 (DE-600)2467241-5 22149414 nnns volume:27 year:2016 pages:517-525 https://doi.org/10.1016/j.jff.2016.10.012 kostenfrei https://doaj.org/article/dca3d6c8541c45e5808fd66405f11332 kostenfrei http://www.sciencedirect.com/science/article/pii/S1756464616303255 kostenfrei https://doaj.org/toc/1756-4646 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_150 GBV_ILN_151 GBV_ILN_165 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_370 GBV_ILN_602 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_2056 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_2098 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_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4251 GBV_ILN_4305 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_4338 GBV_ILN_4393 GBV_ILN_4700 AR 27 2016 517-525
language	English
source	In Journal of Functional Foods 27(2016), Seite 517-525 volume:27 year:2016 pages:517-525
sourceStr	In Journal of Functional Foods 27(2016), Seite 517-525 volume:27 year:2016 pages:517-525
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Alzheimer's disease (AD) β-secretase (BACE1) β-amyloid peptide Paeonia lactiflora Pall 4-O-galloylalbiflorin Docking Nutrition. Foods and food supply
isfreeaccess_bool	true
container_title	Journal of Functional Foods
authorswithroles_txt_mv	Xiao-Long Hu @@aut@@ Ye-Bo Li @@aut@@ Song Qi @@aut@@ Qiao Zhang @@aut@@ Tian-Shu Ren @@aut@@ Wei-Hong Meng @@aut@@ Qing-Chun Zhao @@aut@@
publishDateDaySort_date	2016-01-01T00:00:00Z
hierarchy_top_id	587138432
id	DOAJ073546100
language_de	englisch
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callnumber-first	T - Technology
author	Xiao-Long Hu
spellingShingle	Xiao-Long Hu misc TX341-641 misc Alzheimer's disease (AD) misc β-secretase (BACE1) misc β-amyloid peptide misc Paeonia lactiflora Pall misc 4-O-galloylalbiflorin misc Docking misc Nutrition. Foods and food supply 4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor
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topic_title	TX341-641 4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor Alzheimer's disease (AD) β-secretase (BACE1) β-amyloid peptide Paeonia lactiflora Pall 4-O-galloylalbiflorin Docking
topic	misc TX341-641 misc Alzheimer's disease (AD) misc β-secretase (BACE1) misc β-amyloid peptide misc Paeonia lactiflora Pall misc 4-O-galloylalbiflorin misc Docking misc Nutrition. Foods and food supply
topic_unstemmed	misc TX341-641 misc Alzheimer's disease (AD) misc β-secretase (BACE1) misc β-amyloid peptide misc Paeonia lactiflora Pall misc 4-O-galloylalbiflorin misc Docking misc Nutrition. Foods and food supply
topic_browse	misc TX341-641 misc Alzheimer's disease (AD) misc β-secretase (BACE1) misc β-amyloid peptide misc Paeonia lactiflora Pall misc 4-O-galloylalbiflorin misc Docking misc Nutrition. Foods and food supply
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title	4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor
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title_full	4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor
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title_sort	4-o-galloylalbiflorin discovered from paeonia lactiflora pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (bace1) inhibitor
callnumber	TX341-641
title_auth	4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor
abstract	β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs.
abstractGer	β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs.
abstract_unstemmed	β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the formation of β-amyloid peptides (Aβ), which are important in the development of Alzheimer's disease. It has been demonstrated that albiflorin can alleviate Aβ aggregation. However, the mechanism behind this effect is unknown. In our previous work, albiflorin and its four analogues were isolated from Paeonia lactiflora Pall. This study aims to investigate the relationship of these four compounds with BACE1. Our results show that the albiflorin analogue 4-O-galloylalbiflorin (4-O-GA) had the strongest BACE1 inhibitory effect and was also selective for BACE1. Furthermore, docking study of BACE1 with these analogues yielded similar results, whereby 4-O-GA treatment caused the greatest decreases in both the generation of Aβ1–42 and Aβ1–40 and in the expression of BACE1 and HIF-1α. Our findings indicate that 4-O-GA exerted significant and selective inhibitory activities against BACE1, potentially providing a useful agent for developing BACE1 inhibitor drugs.
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title_short	4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor
url	https://doi.org/10.1016/j.jff.2016.10.012 https://doaj.org/article/dca3d6c8541c45e5808fd66405f11332 http://www.sciencedirect.com/science/article/pii/S1756464616303255 https://doaj.org/toc/1756-4646
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doi_str	10.1016/j.jff.2016.10.012
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4-O-galloylalbiflorin discovered from Paeonia lactiflora Pall. is a potential β-site amyloid precursor protein cleaving enzyme 1 (BACE1) inhibitor

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