Isolation and identification of a novel anticoagulant peptide from enzymatic hydrolysates of scorpion ( Buthus martensii Karsch) protein

Structural characterization of Mesobuthus martensii Karsch peptides and anti-inflammatory potency evaluation in human vascular endothelial cells

“…11 Mesobuthus martensii Karsch peptides (MMKPs) are a class of molecules that show strong anticoagulant, antithrombotic, and brinolysis activities. [12][13][14] Consequently, identifying the bioactive peptide in Mesobuthus martensii Karsch and exploring the anti-inammation effect will be of great value and signicance. To solve this issue, we isolated and identied MMKPs; we explored their anti-inammatory potency in human umbilical vein endothelial cells (HUVECs) and illustrated the underlying mechanism.…”

Interaction of the synthetic antithrombotic peptide P10 with thrombin: a spectroscopy study

“…1B). 21 Ren et al 22 puried an anticoagulant peptide with the sequence VEPVTVNPHE from Buthus martensii Karsch, which inhibited thrombin activity with an IC 50 of 0.012 mg mL À1 . In addition, three peptides SWAQL, GNHEAGE and CFNEYE were puried from the Alcalase 2.4L hydrolysate of peanut protein, showing complete inhibition of thrombin activity at a concentration of 0.4 mg mL À1 .…”

A Novel Direct Factor Xa Inhibitory Peptide with Anti-Platelet Aggregation Activity from Agkistrodon acutus Venom Hydrolysates

“…Agkistrodon acutus venom (0.4 g) was dissolved in 10 mL of 0.1 M phosphate buffer solution (PBS) (when using neutrase, papain and alcalase) or 0.1 M Glycine-HCl solution (when using pepsin). Then, it was hydrolyzed for 12 h using neutrase at pH 8.0 at 50 °C, alcalase at pH 8.0, 50 °C, pepsin at pH 2.0, 37 °C and papain at pH 6.0, 37 °C with a total enzyme dose of 1% 15 . Aliquots of each hydrolysate were collected at 1 h, 2 h, 3 h, 4 h, 8 h and 12 h and were boiled for 10 min to stop the reaction.…”

“…Some peptides, which are inactive within the parent protein, can be released by enzymatic hydrolysis and exhibit diverse bioactivities. Thus, a number of bioactive peptides have been obtained by enzymatic methods, and those peptides include angiotensin-converting enzyme (ACE) inhibitory peptide from tuna frame protein hydrolysate 12 , antioxidant peptide from grass carp muscle hydrolysate 13 , antimicrobial peptide from anchovy hydrolysate 14 , and anticoagulant peptide from scorpion protein and goby muscle protein hydrolysate 15 16 . However, studies of the hydrolysis of animal venoms are rare.…”