Investigation of the role of disulphide bond in modulating internal motions of BmK AGAP protein by molecular dynamics simulation |
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| Authors: | Yong Cui Shanshan Li Yuna Chen Shikui Hu Yongbo Song He Wang |
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| Institution: | 1. School of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, Shenyang, P.R. China;2. School of Medical Devices, Shenyang Pharmaceutical University, Shenyang, P.R. China;3. School of Medical Devices, Shenyang Pharmaceutical University, Shenyang, P.R. China |
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| Abstract: | Elucidating structural determinants in the functional regions of toxins can provide useful knowledge for designing novel analgesic peptides. A series of 100 ns MD simulations were performed on the scorpion toxin BmK AGAP in native and disulphide bond broken states. The comparison of disulphide bond broken states with the native state showed the α-helix was found to be the key to the analgesic activity. Furthermore, our results revealed disulphide bonds have considerable influence on the functionally important essential modes of motions and the correlations between the motions of the Core domain and the C-terminal region which are involved in the analgesic activity. Therefore, we can conclude that disulphide bonds have a crucial role in modulating the function via adjusting the dynamics of scorpion toxin BmK AGAP molecule. |
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| Keywords: | BmK AGAP molecular simulation disulphide bonds molecular dynamics |
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