Metabolite profile and pharmacological relevance of Ortega leaf and fruit extracts.

Ortega is a perennial tropical shrub traditionally used as conventional medicine for the treatment of various ailments. The present study aims to validate the use of Ortega leaf (SVLE) and fruit extracts (SVFE) in traditional medicine through untargeted metabolomics and assessment of its biological and phytochemical properties. GC-MS-based untargeted metabolomics identified derivatives of 59 and 50 metabolites in SVLE and SVFE, respectively.

The wound healing potential of a pro-angiogenic peptide purified from Indian Russell's viper (Daboia russelii) venom.

The cutaneous wound healing property of a pro-angiogenic venom peptide (RVVAP) in a cream-based formulation was evaluated using the excision wound healing model on Wistar strain rats. The wound healing potency and modest antibacterial activity of RVVAP was enhanced significantly (p < 0.05) when combined with Aloe vera extract.

Pathophysiological significance and therapeutic applications of snake venom protease inhibitors.

Protease inhibitors are important constituents of snake venom and play important roles in the pathophysiology of snakebite. Recently, research on snake venom protease inhibitors has provided valuable information to decipher the molecular details of various biological processes and offer insight for the development of some therapeutically important molecules from snake venom. The process of blood coagulation and fibrinolysis, in addition to affecting platelet function, are well known as the major targets of several snake venom protease inhibitors.

Mechanism of apoptosis induction in human breast cancer MCF-7 cell by Ruviprase, a small peptide from Daboia russelii russelii venom.

Ruviprase, a 4.4 kDa peptide isolated from Daboia russelii russelii venom demonstrated antiproliferative activity against EMT6/AR1, U-87MG, HeLa and MCF-7 cancer cells with an IC50 value of 23.0, 8.

Elucidation of procoagulant mechanism and pathophysiological significance of a new prothrombin activating metalloprotease purified from Daboia russelii russelii venom.

The procoagulant proteases present in Russell's Viper venom (RVV) are responsible for promoting consumption coagulopathy in victims. In this study, a procoagulant metalloprotease (Rusviprotease) possessing prothrombin activating and α-fibrinogenase properties has been purified and characterized from RVV. Rusviprotease is a 26.

Biochemical and pharmacological characterization of a toxic fraction and its cytotoxin-like component isolated from Russell's viper (Daboia russelii russelii) venom.

The pathophysiological significance of a toxic fraction (GF-VI DEAE-II) isolated from Russell's viper venom (RVV) is characterized. GF-VI DEAE-II represents 1.6% of the total RVV protein and it comprises of a 27.

Two acidic, anticoagulant PLA2 isoenzymes purified from the venom of monocled cobra Naja kaouthia exhibit different potency to inhibit thrombin and factor Xa via phospholipids independent, non-enzymatic mechanism.

Background: The monocled cobra (Naja kaouthia) is responsible for snakebite fatality in Indian subcontinent and in south-western China. Phospholipase A2 (PLA2; EC 3.1.

A new peptide (Ruviprase) purified from the venom of Daboia russelii russelii shows potent anticoagulant activity via non-enzymatic inhibition of thrombin and factor Xa.

Compounds showing dual inhibition of thrombin and factor Xa (FXa) are the subject of great interest owing to their broader specificity for effective anticoagulation therapy against cardiovascular disorders. This is the first report on the functional characterization and assessment of therapeutic potential of a 4423.6 Da inhibitory peptide (Ruviprase) purified from Daboia russelii russelii venom.

Characterization of a pro-angiogenic, novel peptide from Russell's viper (Daboia russelii russelii) venom.

Present report shows for the first time on the induction of in vitro angiogenesis by a 3.9 kDa novel peptide (RVVAP) purified from Russell's viper venom. Secondary structure of RVVAP is made up of 36.

Bafibrinase: A non-toxic, non-hemorrhagic, direct-acting fibrinolytic serine protease from Bacillus sp. strain AS-S20-I exhibits in vivo anticoagulant activity and thrombolytic potency.

A non-toxic, direct-acting fibrinolytic serine protease (Bafibrinase) demonstrating thrombolytic and anticoagulant properties was purified from Bacillus sp. strain AS-S20-I. Bafibrinase was monomeric, with a molecular mass of 32.

An acidic phospholipase A(2) (RVVA-PLA(2)-I) purified from Daboia russelli venom exerts its anticoagulant activity by enzymatic hydrolysis of plasma phospholipids and by non-enzymatic inhibition of factor Xa in a phospholipids/Ca(2+) independent manner.

A homodimeric acidic PLA(2) (RVVA-PLA(2)-I) of 58.0 kDa molecular weight purified from Russell's viper (Daboia russelli) venom demonstrated dose-dependent catalytic, strong anticoagulant and indirect hemolytic activities and inhibited blood coagulation cascade in both enzymatic and non-enzymatic mechanisms. In in vitro condition, RVVA-PLA(2)-I showed preferential hydrolysis of phosphatidylcholine with a K(m) and V(max) values of 0.