Linked Life Data

20564050

Source:http://linkedlifedata.com/resource/pubmed/id/20564050

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-7-19
pubmed:abstractText
Formation of toxic amyloid structures is believed to be associated with various late-onset neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. The fact that many proteins in addition to those that are associated with clinical conditions have the potential to form amyloid fibrils in vitro provides opportunities for studying the fundamentals of protein aggregation and amyloid formation in model systems. Accordingly, considerable interest and effort has been directed toward developing small molecules to inhibit the formation of fibrillar assemblies and their associated toxicities. In the present study, we investigated the inhibitory effect of crocin and safranal, two principal components of saffron, on fibrillation of apo-alpha-lactalbumin (a-alpha-LA), used as a model protein, under amyloidogenic conditions. In the absence of any ligand, formation of soluble oligomers became evident after 18 h of incubation, followed by subsequent appearance of mature fibrils. Upon incubation with crocin or safranal, while transition phase to monomeric beta structures was not significantly affected, formation of soluble oligomers and following fibrillar assemblies were inhibited. While both safranal and crocin had the ability to bind to hydrophobic patches provided in the intermediate structures, and thereby inhibit protein aggregation, crocin was found more effective, possibly due to its simultaneous hydrophobic and hydrophilic character. Cell viability assay indicated that crocin could diminish toxicity while safranal act in reverse order.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2010 Wiley Periodicals, Inc.
pubmed:issnType
Print
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
854-65
pubmed:meshHeading
pubmed-meshheading:20564050-Amyloid, pubmed-meshheading:20564050-Animals, pubmed-meshheading:20564050-Biological Assay, pubmed-meshheading:20564050-Carotenoids, pubmed-meshheading:20564050-Cattle, pubmed-meshheading:20564050-Circular Dichroism, pubmed-meshheading:20564050-Congo Red, pubmed-meshheading:20564050-Crocus, pubmed-meshheading:20564050-Cyclohexenes, pubmed-meshheading:20564050-Lactalbumin, pubmed-meshheading:20564050-Microscopy, Atomic Force, pubmed-meshheading:20564050-Molecular Weight, pubmed-meshheading:20564050-PC12 Cells, pubmed-meshheading:20564050-Particle Size, pubmed-meshheading:20564050-Protein Structure, Secondary, pubmed-meshheading:20564050-Protein Structure, Tertiary, pubmed-meshheading:20564050-Rats, pubmed-meshheading:20564050-Spectrometry, Fluorescence, pubmed-meshheading:20564050-Terpenes, pubmed-meshheading:20564050-Thiazoles
pubmed:year
2010
pubmed:articleTitle
Fibrillation of alpha-lactalbumin: effect of crocin and safranal, two natural small molecules from Crocus sativus.
pubmed:affiliation
Department of Cell and Molecular Biology, Faculty of Science, University of Tehran, and Shariati Hospital, Tehran, Iran.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't