Linked Life Data

17451866

Source:http://linkedlifedata.com/resource/pubmed/id/17451866

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
2007-6-5
pubmed:abstractText
The formation of amyloid fibrils from insulin is investigated using drop-coating-deposition-Raman (DCDR) difference spectroscopy and atomic force microscopy (AFM). Fibrils formed using various co-solvents and heating cycles are found to induce the appearance of Raman difference peaks in the amide I (approximately 1675 cm(-1)), amide III (approximately 1220 cm(-1)), and peptide backbone (approximately 1010 cm(-1)), consistent with an increase in beta-sheet content. Comparisons of results obtained from fibrils in either H2O or D2O suggest that the NH/ND stretch bands (at approximately 3300 cm(-1)/ approximately 2400 cm(-1)) are also enhanced in intensity upon fibril formation. If there is any water trapped in the core of the fibrils its OH/OD Raman intensity is too small to be detected in the presence of the stronger NH/ND bands which appear in the same region. AFM is used to confirm the formation of fibrils of about 5 nm diameter (and various lengths).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
128
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
150-5
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Analysis of insulin amyloid fibrils by Raman spectroscopy.
pubmed:affiliation
Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
pubmed:publicationType
Journal Article