Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-6-11
pubmed:abstractText
Investigations of amyloidogenic diseases use synthetic peptides for cell-free and in vitro studies. However, amyloidogenic peptides often show intrinsic variability that markedly affects the reproducibility of experiments. Proof of physicochemical and biological variability with different batches of amyloidogenic peptides have been reported in literature. Here, we show that differences can be observed even within the same batch of Abeta1-42 peptide after storing lyophilised samples at -20 degrees C. This change (referred to as 'peptide aging') was reproduced with Abeta1-40 peptide samples by using a series of lyophilisation cycles, showing that lyophilisation, rather than preserving the physicochemical and biological features of Abeta peptides, introduces wide variability. To counteract synthetic peptide aging, we set up a procedure involving the sequential use of trifluoroacetic acid, formic acid and sodium hydroxide solutions that disaggregate preformed seeds and enriched Abeta peptide solutions into monomers and low-molecular-weight oligomers. This procedure enabled us to obtain reproducible physicochemical and biological features of Abeta peptides, irrespective of their age.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1744-2818
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-80
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Overcoming synthetic Abeta peptide aging: a new approach to an age-old problem.
pubmed:affiliation
Department of Biochemistry and Molecular Pharmacology, Mario Negri Institute for Pharmacological Research, Milan, Italy. manzoni@marionegri.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't