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Functional proteomic analysis of Ankaferd® Blood Stopper
Duygu Özel Demiralp1, İbrahim C Haznedaroglu, Nejat Akar
1Proteomics Unit, Ankara University Biotechnology Institute, 06100 Ankara, Turkey Phone: +90 312 222 58 17 - +90 312 222 58 26
Summary
Ankaferd® Blood Stopper (ABS) utilizes a plant-based protein network to stop bleeding by aggregating red blood cells. Proteomic analysis identified plant and human-like proteins, supporting its hemostatic effects.
Area of Science:
- Biochemistry
- Proteomics
- Pharmacology
Background:
- Ankaferd® Blood Stopper (ABS) is a plant-derived hemostatic agent.
- Its mechanism involves forming a protein network for erythrocyte aggregation, influencing primary and secondary hemostasis without altering coagulation factors.
Purpose of the Study:
- To elucidate the effect mechanisms of ABS on hemostasis.
- To identify the specific plant and human-like proteins present in ABS.
Main Methods:
- Proteomic analysis was conducted using 2D gel electrophoresis and mass spectrometry.
- Functional proteomic studies were performed to analyze protein interactions.
Main Results:
- Plant-derived proteins identified include NADP-dependent-malic enzyme, ribulose bisphosphate-carboxylase-large chain, and ATP synthase subunits.
- Human-like peptides detected in ABS include ATP synthase, mucin-16, dynactin 5, and various actin-binding proteins.
Conclusions:
- Proteomic analysis provides a foundation for further research into ABS.
- Future studies will focus on ABS's wound healing, hemostatic, anti-infective, antineoplastic, and preservative properties.
