| DOI | Resolve DOI: https://doi.org/10.1139/v94-186#.WEmiobIrJhE |
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| Author | Search for: Wennerberg, Anders B. A.; Search for: Jackson, Michael1; Search for: Öhman, Anders; Search for: Gräslund, Astrid; Search for: Langel, Ülo; Search for: Bartfai, Tamas; Search for: Rigler, Rudolf; Search for: Mantsch, Henry H.1 |
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| Affiliation | - National Research Council of Canada. NRC Institute for Biodiagnostics
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| Format | Text, Article |
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| Abstract | FT-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. |
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| Publication date | 1994 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | NRC-IBD-48 |
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| NPARC number | 9742318 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 4c26d11a-8da5-4b06-a949-51f54e35c76f |
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| Record created | 2009-07-17 |
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| Record modified | 2020-04-27 |
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