Arginine Residues in the C-terminal and their Relationship with the Analgesic Activity of the Toxin from the Chinese Scorpion Buthus martensii Karsch (BmK AGP-SYPU1) |
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Authors: | Yu Wang Yong-Bo Song Guang-Zhao Yang Yong Cui Yong-Shan Zhao Yan-Feng Liu Yan Ma Chun-Fu Wu Jing-Hai Zhang |
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Affiliation: | 1. School of Life Science and Bio-Pharmaceutics, Shenyang Pharmaceutical University, P.O. Box 17, 103 Wenhua Road, Shenhe District, Shenyang, Liaoning Province, 110016, People??s Republic of China 3. The 463rd Hospital of PLA, Shenyang, Liaoning Province, 110042, People??s Republic of China 2. The General Hospital of Shen Yang Military Command, Shenyang, Liaoning Province, 110016, People??s Republic of China
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Abstract: | In this study, we investigated the functional role of arginines in the C-terminal (65?C67) of BmK AGP-SYPU1, an analgesic peptide from the Chinese scorpion Buthus martensii Karsch. Using site-directed mutagenesis, arginines at the C-terminal (65?C66) were deleted or added to the C-terminal (67). The genes for three mutants of BmK AGP-SYPU1 were obtained by PCR. An analgesic activity assay was used to evaluate the role of arginine residues in the analgesic activity. The three-dimensional structure of BmK AGP-SYPU1 was established by homology modeling. As a result, we showed that the arginines in the C-terminal are crucial for the analgesic activity and may be located at analgesic functional sites. Our work has implications for further modification of scorpion toxins to obtain new analgesic peptides with enhanced activity. |
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