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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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Abstract

In this study, we investigated the functional role of arginines in the C-terminal (65–67) of BmK AGP-SYPU1, an analgesic peptide from the Chinese scorpion Buthus martensii Karsch. Using site-directed mutagenesis, arginines at the C-terminal (65–66) 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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Notes

  1. GenBank accession no. Gu726488

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Acknowledgments

This work was supported by the grants from the National Natural Science Foundation of China (no. 30901872), Major Drug Innovation of Liaoning Province (no. 2009ZX09301-012), Natural Science Foundation of Liaoning Province (no. 20082060), Science and Technology Bureau of Shenyang City for Key Laboratory Construction of Pharmaceutical Biotechnology (no. 1081102-1-00), Doctoral Program of Higher special fund (no. 20112134120008).

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Correspondence to Jing-Hai Zhang.

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Wang, Y., Song, YB., Yang, GZ. et al. 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). Appl Biochem Biotechnol 168, 247–255 (2012). https://doi.org/10.1007/s12010-012-9768-7

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