We've updated our Privacy Policy to make it clearer how we use your personal data.
We use cookies to provide you with a better experience, read our Cookie Policy
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: 672
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: 672
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.
Ask the author a question about this poster.
This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License.
Related Posters
CCS-centric protein identification using IM Score
Robin Park1, Patrick Garrett3, Sven Brehmer2, Titus Jung3, Vijayaraja Gnanasambandan1, Marc-Antoine Beauvais1, Sebastian Wehner2, Lennard Pfennig2, Hyunsoo Kim3, Christopher Adams1, Dennis Trede2, John R. Yates, III3, Rohan Thakur1 1Bruker Daltonics Inc., USA 2Bruker Daltonik GmbH, Bremen, Germany 3Scripps Research, San Diego, USA
Real-time search of Ubiquitin diGLY modified peptides and PaSER acquisition control on the timsTOF PRO
Christopher Adams1; Robin Park1; Nagarjuna Nagaraj4; Sven Brehmer4; Matt Willetts3; Elizabeth Gordon3; Barry M. Zee2; Hayley Peckham2; Kimberly Lee2; Tharan Srikumar3 1Bruker,San Jose,CA;2Cell Signaling Technologies, Danvers, MA;3Bruker, Billerica, MA; 4Bruker, Bremen, Germany
Mass Spectrometry
Alfa Chemistry Testing Lab
Targeted Dereplication of Microbial Natural Products by High-Resolution MS and Predicted LC Retention Time
Chervin J,1 Stierhof M,1 Tong MH,1 Peace D,1 Hansen KØ,2 Urgast DS,1 Andersen JH,2 Yu Y,3 Ebel R,1 Kyeremeh K,4 Paget V,5 Cimpan G,5 Van Wyk A,5 McKee M,5 Deng H,1 Jaspars M,1 Tabudravu JN1
Efficient Management of Extractable & Leachable Data in Process Development
Sanji K. Bhal, Joe DiMartino