Fibrin – Fibrinogen scaffold structural modification by phytochemicals and phytoproteases contained in an aqueous extract of Ageratum conyzoides Linn

• Published in: International Journal of Biological and Chemical Sciences Vol. 15; no. 1; pp. 1 - 11
• Main Authors: Akpalo, Amivi Edefia, Awaga, Kwami Lumo, Tete-Benissan, Amivi Kafui
• Format: Journal Article
• Language: English
• Published: 21.04.2021
• ISSN: 1991-8631; 1997-342X
• DOI: 10.4314/ijbcs.v15i1.1

Based on mechanisms of fibrin clot polymerization and dissolution, it is possible to modulate fibrin formation and removal. Ageratum conyzoides Linn. (Asteraceae) is an annual herb with a long history of traditional medicine. There is high variability in the secondary metabolites of this plant which include flavonoids, and these molecules belong to a class of serine proteases inhibitors. Several plant enzymes belonging to the classes of serine proteases were observed to be active on the cascade of coagulation pathways. The aim of this study was to observe if even Ageratum conyzoides Linn. aqueous leaves extract contained proteases which could structurally modify the fibrin clot formation. To prepare plant extracts, dry leaves of the plant were extracted with distilled water. Fibrin gels were prepared by mixtures containing fibrinogen and thrombin with or without extract. Fibrin networks were disrupted by a denaturation buffer. Samples were deposited in 8% polyacrylamide gel and Coomassie blue was used to reveal migration. Our extract contained phytochemicals class flavonoids which are thrombin inhibitors. But our results support the evidence that the same extract contained plant serine proteases, specifically a fibrinogenase which hydrolyzed fibrinogen but not like thrombin.Keywords: Fibrin/Fibrinogen, structural modification, Ageratum conyzoides Linn., phytoproteases.