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DC Field | Value | Language |
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dc.contributor.author | Jackson, Graham E. | - |
dc.contributor.author | Gamieldien, Riedaa | - |
dc.contributor.author | Mugumbate, Grace | - |
dc.contributor.author | Gäde, Gerd | - |
dc.date.accessioned | 2022-06-28T12:30:59Z | - |
dc.date.available | 2022-06-28T12:30:59Z | - |
dc.date.issued | 2014 | - |
dc.identifier.issn | 0196-9781 | - |
dc.identifier.uri | https://doi.org/10.1016/j.peptides.2013.12.019 | - |
dc.identifier.uri | http://hdl.handle.net/11408/4925 | - |
dc.description.abstract | Melme-CC (pGlu-Leu-Asn-Tyr-Ser-Pro-Asp-Trp amide) and Declu-CC (pGlu-Leu-Asn-Phe-Ser-Pro-Asn-Trp-Gly-Asn amide) are members of the insect adipokinetic hormone family with very different activities in the locust bioassay. The conformations of both peptides were determined in water and in a phospholipid (DPC) micelle solution using nuclear magnetic resonance (NMR) restrained molecular dynamics simulations. In water, Melme-CC has one dominant conformation while in DPC solution it has two preferred conformation. In water, Declu-CC has two conformations but in DPC solution it has one preferred conformation, which is similar to one of the water conformations. All the conformations have type IV β-turn between residues 4 and 7. The binding of the two peptides to the DPC micelle is different. Melme-CC does not bind strongly to the surface and is oriented with the β-turn facing the surface. Declu-CC interacts more strongly with the β-turn facing away from the surface. Both termini having hydrophobic interactions with the surface. In Declu-CC the side chain of Asn7 projects away from the chain while in Melme-CC the Asp7 side chain is folded inside the chain. The different orientation of these side chains may account for the much higher biological activity of Declu-CC in mobilizing lipids in the locust compared to the poor biological effect of Melme-CC in this bioassay. Receptor binding of Declu-CC was tested using a model AKH receptor from Anopheles gambiae. A free energy of binding of −38.5 kJ mol−1 was found. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.ispartofseries | Peptides;Volume 53, Pages 270-277 | - |
dc.subject | Adipokinetic hormones (AKHs) | en_US |
dc.subject | Melme-CC | en_US |
dc.subject | Declu-CC | en_US |
dc.subject | Molecular dynamics simulations and receptor docking receptor docking | en_US |
dc.title | Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics | en_US |
dc.type | Article | en_US |
item.openairetype | Article | - |
item.languageiso639-1 | en | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
item.grantfulltext | open | - |
Appears in Collections: | Research Papers |
Files in This Item:
File | Description | Size | Format | |
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Structural studies of adipokinetic hormones in water.pdf | Abstract | 67.58 kB | Adobe PDF | View/Open |
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