The structure of the rodent and porcine neuropeptide galanin and antagonists as determined by FTIR and CD spectroscopy

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DOIResolve DOI: http://doi.org/10.1139/v94-186#.WEmiobIrJhE
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TypeArticle
Journal titleCanadian Journal of Chemistry
ISSN0008-4042
1480-3291
Volume72
Issue6
Pages14951499; # of pages: 5
AbstractFT-IR spectroscopy was used to study the conformation of the porcine neuropeptide galanin, fragments 1−16 of the porcine and human peptides and the antagonists M15 and M35. All peptides were shown to be structureless in aqueous solution. Upon addition to SDS micelles, only porcine galanin and the fragment consisting of amino acids 1−16 showed any evidence of interaction, adopting a helical structure. No interaction could be demonstrated with zwitterionic lipids for any peptide except M15 which formed a thermally unstable helical conformation which unfolded promoting aggregation at around 45 °C.Additional studies on rat galanin in various solvent systems were made by using circular dichroism spectroscopy. The results obtained support the observations made by FT-IR spectroscopy.
Publication date
PublisherCanadian Science Publishing
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biodiagnostics
Peer reviewedYes
NRC number48
NPARC number9742318
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Record identifier4c26d11a-8da5-4b06-a949-51f54e35c76f
Record created2009-07-17
Record modified2016-12-08
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