Linked Life Data

12648928

Source:http://linkedlifedata.com/resource/pubmed/id/12648928

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-3-21
pubmed:abstractText
A convenient way to study lipid oxidation products-modified proteins by means of suitable model systems has been investigated. As a model peptide, the oxidized B chain of insulin has been chemically modified by either 4-hydroxy-2-nonenal (HNE) or hexanal and the extent, sites, and structure of modifications were assessed by electrospray mass spectrometry. A reduction step, using either NaCNBH(3) or NaBH(4), was also studied to stabilize the alkylated compounds. From the data gathered, it appeared that NaCNBH(3), when added at the beginning of incubation, dramatically influenced the HNE-induced modifications in terms of the addition mechanism (Schiff base formation instead of Michael addition) but also of the amino acid residues modified (N-terminal amino acid instead of histidine residues). However, by reducing the HNE-adducted species at the end of the reaction with NaBH(4), the fragment ions obtained in the product ion scan experiments become more stable and thus, easier to interpret in terms of origin and mechanism involved. With regard to hexanal induced modifications, we have observed that hexanal addition under reductive conditions led to an extensive modification of the peptide backbone. Moreover, as confirmed by "in-source" collision followed by collision induced dissociation (CID) experiments on selected precursor ions (pseudo-MS(3) experiments), N,N-di-alkylations were first observed on the N-terminal residue and further on Lys(29) residue. On the other hand, compared to the native peptide, no significant changes in MS/MS fragmentation patterns (b and y ions series) were observed whatever the basic site modified by the aldehyde-addition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1044-0305
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
215-26
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Study of protein modification by 4-hydroxy-2-nonenal and other short chain aldehydes analyzed by electrospray ionization tandem mass spectrometry.
pubmed:affiliation
Department of Quality and Safety Assurance, Nestlé Research Center, Nestec Ltd., Lausanne, Switzerland.
pubmed:publicationType
Journal Article