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Article: Salvianolic acid B inhibits Aβ fibril formation and disaggregates preformed fibrils and protects against Aβ-induced cytotoxicty

TitleSalvianolic acid B inhibits Aβ fibril formation and disaggregates preformed fibrils and protects against Aβ-induced cytotoxicty
Authors
Keywordsβ-Amyloid fibrils
Aβ aggregating ELISA
Alzheimer's disease
Circular dichroism spectroscopy
Cytotoxicity
Electron microscopy
Salvianolic acid B
Thioflavine T
Issue Date2008
PublisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/neuint
Citation
Neurochemistry International, 2008, v. 52 n. 4-5, p. 741-750 How to Cite?
AbstractOne of the major pathological features of Alzheimer's disease (AD) is the appearance of senile plaques characterized by extracellular aggregation of amyloid β-peptide (Aβ) fibrils. Inhibition of Aβ fibril aggregation is therefore viewed as one possible method to halt the progression of AD. Salvianolic acid B (Sal B) is an active ingredient isolated from Salvia miltiorrhiza, a Chinese herbal medicine commonly used for the treatment of cardiovascular and cerebrovascular disorders. Recent findings show that Sal B prevents Aβ-induced cytotoxicity in a rat neural cell line. To understand the mechanism of Sal B-mediated neuroprotection, its effects on the inhibition of Aβ1-40 fibril formation and destabilization of the preformed Aβ1-40 fibrils were studied. The results were obtained using Thioflavin T fluorescence assay and Aβ aggregating immunoassay. We found that Sal B can inhibit fibril aggregation (IC50: 1.54-5.37 μM) as well as destabilize preformed Aβ fibril (IC50: 5.00-5.19 μM) in a dose- and time-dependent manner. Sal B is a better aggregation inhibitor than ferulic acid but less active than curcumin in the inhibition of Aβ1-40 aggregation. In electron microscope study, Sal B-treated Aβ1-40 fibrils are seen in various stages of shortening or wrinkling with numerous deformed aggregates of amorphous structure. Circular dichroism data indicate that Sal B dose dependently prevents the formation of β-structured aggregates of Aβ1-40. Addition of preincubated Sal B with Aβ1-42 significantly reduces its cytotoxic effects on human neuroblastoma SH-SY5Y cells. These results suggest that Sal B has therapeutic potential in the treatment of AD, and warrant its study in animal models. © 2007 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68014
ISSN
2023 Impact Factor: 4.4
2023 SCImago Journal Rankings: 1.049
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorDurairajan, SSKen_HK
dc.contributor.authorYuan, Qen_HK
dc.contributor.authorXie, Len_HK
dc.contributor.authorChan, WSen_HK
dc.contributor.authorKum, WFen_HK
dc.contributor.authorKoo, Ien_HK
dc.contributor.authorLiu, Cen_HK
dc.contributor.authorSong, Yen_HK
dc.contributor.authorHuang, JDen_HK
dc.contributor.authorKlein, WLen_HK
dc.contributor.authorLi, Men_HK
dc.date.accessioned2010-09-06T06:00:31Z-
dc.date.available2010-09-06T06:00:31Z-
dc.date.issued2008en_HK
dc.identifier.citationNeurochemistry International, 2008, v. 52 n. 4-5, p. 741-750en_HK
dc.identifier.issn0197-0186en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68014-
dc.description.abstractOne of the major pathological features of Alzheimer's disease (AD) is the appearance of senile plaques characterized by extracellular aggregation of amyloid β-peptide (Aβ) fibrils. Inhibition of Aβ fibril aggregation is therefore viewed as one possible method to halt the progression of AD. Salvianolic acid B (Sal B) is an active ingredient isolated from Salvia miltiorrhiza, a Chinese herbal medicine commonly used for the treatment of cardiovascular and cerebrovascular disorders. Recent findings show that Sal B prevents Aβ-induced cytotoxicity in a rat neural cell line. To understand the mechanism of Sal B-mediated neuroprotection, its effects on the inhibition of Aβ1-40 fibril formation and destabilization of the preformed Aβ1-40 fibrils were studied. The results were obtained using Thioflavin T fluorescence assay and Aβ aggregating immunoassay. We found that Sal B can inhibit fibril aggregation (IC50: 1.54-5.37 μM) as well as destabilize preformed Aβ fibril (IC50: 5.00-5.19 μM) in a dose- and time-dependent manner. Sal B is a better aggregation inhibitor than ferulic acid but less active than curcumin in the inhibition of Aβ1-40 aggregation. In electron microscope study, Sal B-treated Aβ1-40 fibrils are seen in various stages of shortening or wrinkling with numerous deformed aggregates of amorphous structure. Circular dichroism data indicate that Sal B dose dependently prevents the formation of β-structured aggregates of Aβ1-40. Addition of preincubated Sal B with Aβ1-42 significantly reduces its cytotoxic effects on human neuroblastoma SH-SY5Y cells. These results suggest that Sal B has therapeutic potential in the treatment of AD, and warrant its study in animal models. © 2007 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/neuinten_HK
dc.relation.ispartofNeurochemistry Internationalen_HK
dc.rightsNeurochemistry International. Copyright © Elsevier Ltd.en_HK
dc.subjectβ-Amyloid fibrils-
dc.subjectAβ aggregating ELISA-
dc.subjectAlzheimer's disease-
dc.subjectCircular dichroism spectroscopy-
dc.subjectCytotoxicity-
dc.subjectElectron microscopy-
dc.subjectSalvianolic acid B-
dc.subjectThioflavine T-
dc.subject.meshAmyloid beta-Peptides - antagonists & inhibitors - biosynthesis - toxicityen_HK
dc.subject.meshAntioxidants - pharmacologyen_HK
dc.subject.meshBenzofurans - pharmacologyen_HK
dc.subject.meshCell Aggregation - drug effectsen_HK
dc.subject.meshCell Line, Tumoren_HK
dc.subject.meshCircular Dichroismen_HK
dc.subject.meshData Interpretation, Statisticalen_HK
dc.subject.meshEnzyme-Linked Immunosorbent Assayen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMicrofibrils - drug effects - ultrastructureen_HK
dc.subject.meshMicroscopy, Electronen_HK
dc.subject.meshTetrazolium Saltsen_HK
dc.subject.meshThiazoles - pharmacologyen_HK
dc.titleSalvianolic acid B inhibits Aβ fibril formation and disaggregates preformed fibrils and protects against Aβ-induced cytotoxictyen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0197-0186&volume=52&spage=741&epage=750&date=2008&atitle=Salvianolic+acid+B+inhibits+Aβ+fibril+formation+and+disaggregates+preformed+fibrils+and+protects+against+Aβ-induced+cytotoxicty+en_HK
dc.identifier.emailSong, Y:songy@hkucc.hku.hken_HK
dc.identifier.emailHuang, JD:jdhuang@hkucc.hku.hken_HK
dc.identifier.authoritySong, Y=rp00488en_HK
dc.identifier.authorityHuang, JD=rp00451en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.neuint.2007.09.006en_HK
dc.identifier.pmid17964692-
dc.identifier.scopuseid_2-s2.0-38349160407en_HK
dc.identifier.hkuros145499en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-38349160407&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume52en_HK
dc.identifier.issue4-5en_HK
dc.identifier.spage741en_HK
dc.identifier.epage750en_HK
dc.identifier.isiWOS:000254968300026-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridDurairajan, SSK=23469201000en_HK
dc.identifier.scopusauthoridYuan, Q=7202814773en_HK
dc.identifier.scopusauthoridXie, L=23483050700en_HK
dc.identifier.scopusauthoridChan, WS=35101583400en_HK
dc.identifier.scopusauthoridKum, WF=15063144400en_HK
dc.identifier.scopusauthoridKoo, I=23469778400en_HK
dc.identifier.scopusauthoridLiu, C=24503690100en_HK
dc.identifier.scopusauthoridSong, Y=7404921212en_HK
dc.identifier.scopusauthoridHuang, JD=8108660600en_HK
dc.identifier.scopusauthoridKlein, WL=7402435293en_HK
dc.identifier.scopusauthoridLi, M=36071647500en_HK
dc.identifier.issnl0197-0186-

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