An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity

Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. He...
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Gespeichert in:

Autor*in:	Tao Jin [verfasserIn] Weishuai Lian [verfasserIn] Xiaojun Zhang [verfasserIn] Shuqing Wang [verfasserIn] Minjie Xu [verfasserIn] Amir Sherchan [verfasserIn] Maoquan Li [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	Amyloid β Salidroside Cerebrovascular endothelial cell

Übergeordnetes Werk:	In: Arabian Journal of Chemistry - Elsevier, 2016, 16(2023), 4, Seite 104548-
Übergeordnetes Werk:	volume:16 ; year:2023 ; number:4 ; pages:104548-

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.arabjc.2023.104548

Katalog-ID:	DOAJ080567789

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520			\|a Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases.
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publishDate	2023
allfields	10.1016/j.arabjc.2023.104548 doi (DE-627)DOAJ080567789 (DE-599)DOAJ2c9064df68aa4336a21f2b080f5c5058 DE-627 ger DE-627 rakwb eng QD1-999 Tao Jin verfasserin aut An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases. Amyloid β Salidroside Cerebrovascular endothelial cell Chemistry Weishuai Lian verfasserin aut Xiaojun Zhang verfasserin aut Shuqing Wang verfasserin aut Minjie Xu verfasserin aut Amir Sherchan verfasserin aut Maoquan Li verfasserin aut In Arabian Journal of Chemistry Elsevier, 2016 16(2023), 4, Seite 104548- (DE-627)609401564 (DE-600)2515214-2 18785352 nnns volume:16 year:2023 number:4 pages:104548- https://doi.org/10.1016/j.arabjc.2023.104548 kostenfrei https://doaj.org/article/2c9064df68aa4336a21f2b080f5c5058 kostenfrei http://www.sciencedirect.com/science/article/pii/S1878535223000096 kostenfrei https://doaj.org/toc/1878-5352 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 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_2034 GBV_ILN_2038 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_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 16 2023 4 104548-
spelling	10.1016/j.arabjc.2023.104548 doi (DE-627)DOAJ080567789 (DE-599)DOAJ2c9064df68aa4336a21f2b080f5c5058 DE-627 ger DE-627 rakwb eng QD1-999 Tao Jin verfasserin aut An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases. Amyloid β Salidroside Cerebrovascular endothelial cell Chemistry Weishuai Lian verfasserin aut Xiaojun Zhang verfasserin aut Shuqing Wang verfasserin aut Minjie Xu verfasserin aut Amir Sherchan verfasserin aut Maoquan Li verfasserin aut In Arabian Journal of Chemistry Elsevier, 2016 16(2023), 4, Seite 104548- (DE-627)609401564 (DE-600)2515214-2 18785352 nnns volume:16 year:2023 number:4 pages:104548- https://doi.org/10.1016/j.arabjc.2023.104548 kostenfrei https://doaj.org/article/2c9064df68aa4336a21f2b080f5c5058 kostenfrei http://www.sciencedirect.com/science/article/pii/S1878535223000096 kostenfrei https://doaj.org/toc/1878-5352 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 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_2034 GBV_ILN_2038 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_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 16 2023 4 104548-
allfields_unstemmed	10.1016/j.arabjc.2023.104548 doi (DE-627)DOAJ080567789 (DE-599)DOAJ2c9064df68aa4336a21f2b080f5c5058 DE-627 ger DE-627 rakwb eng QD1-999 Tao Jin verfasserin aut An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases. Amyloid β Salidroside Cerebrovascular endothelial cell Chemistry Weishuai Lian verfasserin aut Xiaojun Zhang verfasserin aut Shuqing Wang verfasserin aut Minjie Xu verfasserin aut Amir Sherchan verfasserin aut Maoquan Li verfasserin aut In Arabian Journal of Chemistry Elsevier, 2016 16(2023), 4, Seite 104548- (DE-627)609401564 (DE-600)2515214-2 18785352 nnns volume:16 year:2023 number:4 pages:104548- https://doi.org/10.1016/j.arabjc.2023.104548 kostenfrei https://doaj.org/article/2c9064df68aa4336a21f2b080f5c5058 kostenfrei http://www.sciencedirect.com/science/article/pii/S1878535223000096 kostenfrei https://doaj.org/toc/1878-5352 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 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_2034 GBV_ILN_2038 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_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 16 2023 4 104548-
allfieldsGer	10.1016/j.arabjc.2023.104548 doi (DE-627)DOAJ080567789 (DE-599)DOAJ2c9064df68aa4336a21f2b080f5c5058 DE-627 ger DE-627 rakwb eng QD1-999 Tao Jin verfasserin aut An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases. Amyloid β Salidroside Cerebrovascular endothelial cell Chemistry Weishuai Lian verfasserin aut Xiaojun Zhang verfasserin aut Shuqing Wang verfasserin aut Minjie Xu verfasserin aut Amir Sherchan verfasserin aut Maoquan Li verfasserin aut In Arabian Journal of Chemistry Elsevier, 2016 16(2023), 4, Seite 104548- (DE-627)609401564 (DE-600)2515214-2 18785352 nnns volume:16 year:2023 number:4 pages:104548- https://doi.org/10.1016/j.arabjc.2023.104548 kostenfrei https://doaj.org/article/2c9064df68aa4336a21f2b080f5c5058 kostenfrei http://www.sciencedirect.com/science/article/pii/S1878535223000096 kostenfrei https://doaj.org/toc/1878-5352 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 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_2034 GBV_ILN_2038 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_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 16 2023 4 104548-
allfieldsSound	10.1016/j.arabjc.2023.104548 doi (DE-627)DOAJ080567789 (DE-599)DOAJ2c9064df68aa4336a21f2b080f5c5058 DE-627 ger DE-627 rakwb eng QD1-999 Tao Jin verfasserin aut An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases. Amyloid β Salidroside Cerebrovascular endothelial cell Chemistry Weishuai Lian verfasserin aut Xiaojun Zhang verfasserin aut Shuqing Wang verfasserin aut Minjie Xu verfasserin aut Amir Sherchan verfasserin aut Maoquan Li verfasserin aut In Arabian Journal of Chemistry Elsevier, 2016 16(2023), 4, Seite 104548- (DE-627)609401564 (DE-600)2515214-2 18785352 nnns volume:16 year:2023 number:4 pages:104548- https://doi.org/10.1016/j.arabjc.2023.104548 kostenfrei https://doaj.org/article/2c9064df68aa4336a21f2b080f5c5058 kostenfrei http://www.sciencedirect.com/science/article/pii/S1878535223000096 kostenfrei https://doaj.org/toc/1878-5352 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_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_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 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_2034 GBV_ILN_2038 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_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 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_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 16 2023 4 104548-
language	English
source	In Arabian Journal of Chemistry 16(2023), 4, Seite 104548- volume:16 year:2023 number:4 pages:104548-
sourceStr	In Arabian Journal of Chemistry 16(2023), 4, Seite 104548- volume:16 year:2023 number:4 pages:104548-
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Amyloid β Salidroside Cerebrovascular endothelial cell Chemistry
isfreeaccess_bool	true
container_title	Arabian Journal of Chemistry
authorswithroles_txt_mv	Tao Jin @@aut@@ Weishuai Lian @@aut@@ Xiaojun Zhang @@aut@@ Shuqing Wang @@aut@@ Minjie Xu @@aut@@ Amir Sherchan @@aut@@ Maoquan Li @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	609401564
id	DOAJ080567789
language_de	englisch
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callnumber-first	Q - Science
author	Tao Jin
spellingShingle	Tao Jin misc QD1-999 misc Amyloid β misc Salidroside misc Cerebrovascular endothelial cell misc Chemistry An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity
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topic_title	QD1-999 An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity Amyloid β Salidroside Cerebrovascular endothelial cell
topic	misc QD1-999 misc Amyloid β misc Salidroside misc Cerebrovascular endothelial cell misc Chemistry
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title	An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity
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title_full	An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity
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title_sort	in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity
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title_auth	An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity
abstract	Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases.
abstractGer	Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases.
abstract_unstemmed	Protein aggregation and associated amyloid formation is linked with several harmful human pathophysiologies including Alzheimer's, Parkinson's, and cerebrovascular diseases. A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. Hence, salidroside can serve as a potential inhibitor in the therapeutic advancement to combat cerebrovascular diseases.
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title_short	An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity
url	https://doi.org/10.1016/j.arabjc.2023.104548 https://doaj.org/article/2c9064df68aa4336a21f2b080f5c5058 http://www.sciencedirect.com/science/article/pii/S1878535223000096 https://doaj.org/toc/1878-5352
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A potential approach for modulating and exploring amyloid fibrillization is the control of protein self-assembly. Herein, anti-aggregation effects of salidroside, its influence on the kinetics of amyloid fibrillization of Aβ1-42 peptide and its cytotoxicity against cerebrovascular endothelial cells (bEnd.3) were assessed by using a wide range of spectroscopic and cellular techniques. The present outcome of Thioflavin T (ThT) and 8-anilino-1-naphthalenesulfonic acid (ANS) fluorescence, Congo red (CR), and circular dichroism (CD) analyses indicated that salidroside potentially inhibits protein fibril formation. The cellular studies inferred that salidroside protects bEnd.3 cells against Aβ1-42 oligomers -triggered cytotoxicity through modulation of oxidative stress [reactive oxygen species (ROS), superoxide dismutase (SOD) and catalase (CAT) activities] and apoptosis (caspase-3 activity). Therefore, the data signifies the role of salidroside as a promising small molecule in inhibiting Aβ1-42 aggregation and associated cerebrovascular endothelial cell toxicity. 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An in vitro study on probable inhibition of cerebrovascular disease by salidroside as a potent small molecule against induction of protein amyloid fibrils and cytotoxicity

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