Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis
Chemosignals play a crucial role in social and sexual communication among inter- and intra-species. Chemical cues are bound with protein that is present in the pheromones irrespective of sex are commonly called as pheromone binding protein (PBP). In rats, the pheromone compounds are bound with low m...
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| Iaith: | English |
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2014
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| Mynediad Ar-lein: | https://hdl.handle.net/10356/103489 http://hdl.handle.net/10220/20011 |
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| author | Ilayaraja, Renganathan Rajkumar, Ramalingam Rajesh, Durairaj Muralidharan, Arumugam Ramachandran Padmanabhan, Parasuraman Archunan, Govindaraju |
| author2 | Lee Kong Chian School of Medicine (LKCMedicine) |
| author_facet | Lee Kong Chian School of Medicine (LKCMedicine) Ilayaraja, Renganathan Rajkumar, Ramalingam Rajesh, Durairaj Muralidharan, Arumugam Ramachandran Padmanabhan, Parasuraman Archunan, Govindaraju |
| author_sort | Ilayaraja, Renganathan |
| collection | NTU |
| description | Chemosignals play a crucial role in social and sexual communication among inter- and intra-species. Chemical cues are bound with protein that is present in the pheromones irrespective of sex are commonly called as pheromone binding protein (PBP). In rats, the pheromone compounds are bound with low molecular lipocalin protein α2u-globulin (α2u). We reported farnesol is a natural endogenous ligand (compound) present in rat preputial gland as a bound volatile compound. In the present study, an attempt has been made through computational method to evaluating the binding efficiency of α2u with the natural ligand (farnesol) and standard fluorescent molecule (2-naphthol). The docking analysis revealed that the binding energy of farnesol and 2-naphthol was almost equal and likely to share some binding pocket of protein. Further, to extrapolate the results generated through computational approach, the α2u protein was purified and subjected to fluorescence titration and binding assay. The results showed that the farnesol is replaced by 2-naphthol with high hydrophobicity of TYR120 in binding sites of α2u providing an acceptable dissociation constant indicating the binding efficiency of α2u. The obtained results are in corroboration with the data made through computational approach. |
| first_indexed | 2024-10-01T04:27:26Z |
| format | Journal Article |
| id | ntu-10356/103489 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T04:27:26Z |
| publishDate | 2014 |
| record_format | dspace |
| spelling | ntu-10356/1034892022-02-16T16:27:35Z Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis Ilayaraja, Renganathan Rajkumar, Ramalingam Rajesh, Durairaj Muralidharan, Arumugam Ramachandran Padmanabhan, Parasuraman Archunan, Govindaraju Lee Kong Chian School of Medicine (LKCMedicine) DRNTU::Science::Medicine Chemosignals play a crucial role in social and sexual communication among inter- and intra-species. Chemical cues are bound with protein that is present in the pheromones irrespective of sex are commonly called as pheromone binding protein (PBP). In rats, the pheromone compounds are bound with low molecular lipocalin protein α2u-globulin (α2u). We reported farnesol is a natural endogenous ligand (compound) present in rat preputial gland as a bound volatile compound. In the present study, an attempt has been made through computational method to evaluating the binding efficiency of α2u with the natural ligand (farnesol) and standard fluorescent molecule (2-naphthol). The docking analysis revealed that the binding energy of farnesol and 2-naphthol was almost equal and likely to share some binding pocket of protein. Further, to extrapolate the results generated through computational approach, the α2u protein was purified and subjected to fluorescence titration and binding assay. The results showed that the farnesol is replaced by 2-naphthol with high hydrophobicity of TYR120 in binding sites of α2u providing an acceptable dissociation constant indicating the binding efficiency of α2u. The obtained results are in corroboration with the data made through computational approach. Published version 2014-07-02T03:35:19Z 2019-12-06T21:13:46Z 2014-07-02T03:35:19Z 2019-12-06T21:13:46Z 2014 2014 Journal Article Ilayaraja, R., Rajkumar, R., Rajesh, D., Muralidharan, A. R., Padmanabhan, P., & Archunan, G. (2014). Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis. Scientific Reports, 4, 5201-. 2045-2322 https://hdl.handle.net/10356/103489 http://hdl.handle.net/10220/20011 10.1038/srep05201 24903953 en Scientific reports This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License. The images in this article are included in the article's Creative Commons license, unless indicated otherwise in the image credit; if the image is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the image. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/ application/pdf |
| spellingShingle | DRNTU::Science::Medicine Ilayaraja, Renganathan Rajkumar, Ramalingam Rajesh, Durairaj Muralidharan, Arumugam Ramachandran Padmanabhan, Parasuraman Archunan, Govindaraju Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis |
| title | Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis |
| title_full | Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis |
| title_fullStr | Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis |
| title_full_unstemmed | Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis |
| title_short | Evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis |
| title_sort | evaluating the binding efficiency of pheromone binding protein with its natural ligand using molecular docking and fluorescence analysis |
| topic | DRNTU::Science::Medicine |
| url | https://hdl.handle.net/10356/103489 http://hdl.handle.net/10220/20011 |
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