Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics
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 phospholip...
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Elsevier
2022
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| Online Access: | https://doi.org/10.1016/j.peptides.2013.12.019 http://hdl.handle.net/11408/4925 |
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| author | Jackson, Graham E. Gamieldien, Riedaa Mugumbate, Grace Gäde, Gerd |
| author_facet | Jackson, Graham E. Gamieldien, Riedaa Mugumbate, Grace Gäde, Gerd |
| author_sort | Jackson, Graham E. |
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| description | 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. |
| format | Article |
| id | ir-11408-4925 |
| institution | My University |
| language | English |
| publishDate | 2022 |
| publisher | Elsevier |
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| spelling | ir-11408-49252022-06-28T12:30:59Z Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics Jackson, Graham E. Gamieldien, Riedaa Mugumbate, Grace Gäde, Gerd Adipokinetic hormones (AKHs) Melme-CC Declu-CC Molecular dynamics simulations and receptor docking receptor docking 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. 2022-06-28T12:30:59Z 2022-06-28T12:30:59Z 2014 Article 0196-9781 https://doi.org/10.1016/j.peptides.2013.12.019 http://hdl.handle.net/11408/4925 en Peptides;Volume 53, Pages 270-277 open Elsevier |
| spellingShingle | Adipokinetic hormones (AKHs) Melme-CC Declu-CC Molecular dynamics simulations and receptor docking receptor docking Jackson, Graham E. Gamieldien, Riedaa Mugumbate, Grace Gäde, Gerd Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics |
| title | Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics |
| title_full | Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics |
| title_fullStr | Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics |
| title_full_unstemmed | Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics |
| title_short | Structural studies of adipokinetic hormones in water and DPC micelle solution using NMR distance restrained molecular dynamics |
| title_sort | structural studies of adipokinetic hormones in water and dpc micelle solution using nmr distance restrained molecular dynamics |
| topic | Adipokinetic hormones (AKHs) Melme-CC Declu-CC Molecular dynamics simulations and receptor docking receptor docking |
| url | https://doi.org/10.1016/j.peptides.2013.12.019 http://hdl.handle.net/11408/4925 |
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