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EP31019
Poster Title: FXa Anticoagulant Bioactive Proteins Derived from Scorpion Venom
Submitted on 22 Nov 2019
Author(s): Meng Li,1 Yuko P. Y. Lam,1 Peng Chen,2 Remy Gavard,1 Cookson K. C. Chiu,1 Christopher A. Wootton,1 Tomos E. Morgan,1 Qiong Wu,2 Mark P. Barrow,1 Hongzheng Fu,2 Peter B. O’Connor1
Affiliations: 1Department of Chemistry, University of Warwick, Coventry, UK; 2 School of Pharmaceutical Sciences, Peking University, Beijing, China
Poster Views: 1,181
Please be aware that this Poster is viewable on an external site.
Submitted on 22 Nov 2019
Author(s): Meng Li,1 Yuko P. Y. Lam,1 Peng Chen,2 Remy Gavard,1 Cookson K. C. Chiu,1 Christopher A. Wootton,1 Tomos E. Morgan,1 Qiong Wu,2 Mark P. Barrow,1 Hongzheng Fu,2 Peter B. O’Connor1
Affiliations: 1Department of Chemistry, University of Warwick, Coventry, UK; 2 School of Pharmaceutical Sciences, Peking University, Beijing, China
Poster Views: 1,181
Please be aware that this Poster is viewable on an external site.
Abstract: The scorpion Mesobuthus Martensii, is a species widely present in China and has been used in traditional Chinese medicines for thousands of years.1 Venoms from this type of scorpions contain a highly complex mixture of polypeptides which have been proven to be bioactive.2,3 These peptides show a diverse variety of pharmaceutical properties for the treatment of many conditions, such as cardiovascular problems, drug dependence, chronic pain, diabetes, and even tumors.4,5
Thromboembolic disorders are causes of mortality and anticoagulation treatment is central to the management of these fatal diseases. Although there are several anticoagulants that are effective in the prevention and treatment of these thrombotic diseases, there are undesirable side effects. FXa is located at the junction of the intrinsic and extrinsic pathways of coagulation and catalyzes the conversion of prothrombin to thrombin. Therefore, research into novel FXa inhibitors is important in the treatment of thrombotic diseases.Summary: Scorpion venom is a highly complex mixture of proteins which have shown a diverse variety of pharmaceutical properties, some showing inhibition of enzyme factor Xa, preventing blood coagulation. These peptide are known to be heavily modified and cross-linked with multiple
disulphide bonds, making tandem mass spectrometry and comparison with predicted sequences extremely challenging.References: 1. Sridhara, S.; Chakravarthy, A. K.; Kalarani, V.; Reddy, D. C., Diversity and Ecology of Scorpions: Evolutionary Success Through Venom, Springer Singapore: 2016; pp 57-80
2 Ortiz, E.; Gurrola, G. B.; Schwartz, E. F.; Possani, L. D., Toxicon 2015, 93, 125-135.
3. D’Suze, G.; Rosales, A.; Salazar, V.; Sevcik, C., Toxicon 2010, 56 (8), 1497-1505.
4. Xu, X.; Duan, Z.; Di, Z.; He, Y.; Li, J.; Li, Z.; Xie, C.; Zeng, X.; Cao, Z.; Wu, Y.; Liang, S.; Li, W., Journal of Proteomics 2014, 106, 162-180.
5. Guan, R.-J.; Xiang, Y.; He, X.-L.; Wang, C.-G.; Wang, M.; Zhang, Y.; Sundberg, E. J.; Wang, D.-C., Journal of Molecular Biology 2004, 341 (5), 1189-1204.
Thromboembolic disorders are causes of mortality and anticoagulation treatment is central to the management of these fatal diseases. Although there are several anticoagulants that are effective in the prevention and treatment of these thrombotic diseases, there are undesirable side effects. FXa is located at the junction of the intrinsic and extrinsic pathways of coagulation and catalyzes the conversion of prothrombin to thrombin. Therefore, research into novel FXa inhibitors is important in the treatment of thrombotic diseases.Summary: Scorpion venom is a highly complex mixture of proteins which have shown a diverse variety of pharmaceutical properties, some showing inhibition of enzyme factor Xa, preventing blood coagulation. These peptide are known to be heavily modified and cross-linked with multiple
disulphide bonds, making tandem mass spectrometry and comparison with predicted sequences extremely challenging.References: 1. Sridhara, S.; Chakravarthy, A. K.; Kalarani, V.; Reddy, D. C., Diversity and Ecology of Scorpions: Evolutionary Success Through Venom, Springer Singapore: 2016; pp 57-80
2 Ortiz, E.; Gurrola, G. B.; Schwartz, E. F.; Possani, L. D., Toxicon 2015, 93, 125-135.
3. D’Suze, G.; Rosales, A.; Salazar, V.; Sevcik, C., Toxicon 2010, 56 (8), 1497-1505.
4. Xu, X.; Duan, Z.; Di, Z.; He, Y.; Li, J.; Li, Z.; Xie, C.; Zeng, X.; Cao, Z.; Wu, Y.; Liang, S.; Li, W., Journal of Proteomics 2014, 106, 162-180.
5. Guan, R.-J.; Xiang, Y.; He, X.-L.; Wang, C.-G.; Wang, M.; Zhang, Y.; Sundberg, E. J.; Wang, D.-C., Journal of Molecular Biology 2004, 341 (5), 1189-1204.
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