Production of Hyaluronidase by .

Hyaluronidases have been a subject of great interest in medical and cosmeceutical applications. Previously, our group demonstrated that the venom glands of contain hyaluronidase enzymes (VesT2s), and heterologous expression of the corresponding gene () in systems results in inclusion bodies, necessitating functional folding using urea. Here, we report the successful heterologous expression of VesT2a in the expression system, with gene construction achieved using Golden.

Characterization and Localization of Sol g 2.1 Protein from Fire Ant Venom in the Central Nervous System of Injected Crickets ().

is recognized for containing the allergenic proteins Sol g 1, 2, 3, and 4 in its venom. Remarkably, Sol g 2.1 exhibits hydrophobic binding and has a high sequence identity (83.

Inhibitory Effect of Isopanduratin A on Adipogenesis: A Study of Possible Mechanisms.

The root of , a culinary plant commonly known as fingerroot, has previously been reported to possess anti-obesity activity, with four flavonoids identified as active principles, including pinostrobin, panduratin A, cardamonin, and isopanduratin A. However, the molecular mechanisms underlying the antiadipogenic potential of isopanduratin A remain unknown. In this study, isopanduratin A at non-cytotoxic concentrations (1-10 μM) significantly suppressed lipid accumulation in murine (3T3-L1) and human (PCS-210-010) adipocytes in a dose-dependent manner.

In Silico and In Vitro Structure-Activity Relationship of Mastoparan and Its Analogs.

Antimicrobial peptides are an important class of therapeutic agent used against a wide range of pathogens such as Gram-negative and Gram-positive bacteria, fungi, and viruses. Mastoparan (MpVT) is an α-helix and amphipathic tetradecapeptide obtained from venom. This peptide exhibits antibacterial activity.

Novel Antimicrobial Peptides from a Cecropin-Like Region of Heteroscorpine-1 from Venom with Membrane Disruption Activity.

The increasing antimicrobial-resistant prevalence has become a severe health problem. It has led to the invention of a new antimicrobial agent such as antimicrobial peptides. Heteroscorpine-1 is an antimicrobial peptide that has the ability to kill many bacterial strains.

Anti-metastatic Effects of Cationic KT2 Peptide (a Lysine/Tryptophan-rich Peptide) on Human Melanoma A375.S2 Cells.

Background/aim: KT2 is a lysine/tryptophan-rich peptide modified from Crocodylus siamensis Leucrocin I. In this study, we examined the cell toxicity, cellular uptake, anti-migration and anti-invasion activities of KT2 in A375.S2 human melanoma cells.

Heterologous expression and mutagenesis of recombinant hyaluronidase protein (rVesA2).

Background: Crude venom of the banded tiger wasp contains a variety of enzymes including hyaluronidases, commonly known as spreading factors.

Methods: The cDNA cloning, sequence analysis and structural modelling of venom hyaluronidase (VesA2) were herein described. Moreover, heterologous expression and mutagenesis of rVesA2 were performed.

Purification and biochemical characterization of VesT1s, a novel phospholipase A1 isoform isolated from the venom of the greater banded wasp Vespa tropica.

Vespa tropica, a social wasp locally found in Thailand is responsible for many out off the record accidental stings due to close encounters with human activities and because of the animal's highly potent venom. Phospholipase (PLA) is one of the major proteins commonly found in insect venom. In this work, V.

Cloning, structural modelling and characterization of VesT2s, a wasp venom hyaluronidase (HAase) from .

Background: Wasp venom is a complex mixture containing proteins, enzymes and small molecules, including some of the most dangerous allergens. The greater banded wasp () is well-known for its lethal venom, whose one of the major components is a hyaluronidase (HAase). It is believed that the high protein proportion and activity of this enzyme is responsible for the venom potency.

Comparative proteomic analysis of two wasps venom, Vespa tropica and Vespa affinis.

Vespid venom is composed of many bioactive compounds. The venom of the banded tiger wasp (Vespa affinis, or VA) and the great banded wasp (Vespa tropica, or VT)-which are locally found in the northeastern part of Thailand and are well known for their life-threatening venom potency-were comparatively studied in terms of potency, composition and biological activity. Clinical studies that included word-of-mouth information shared by traditional healers in local areas noted that the venom of VT is more potent than that of VA.

Purification and structural characterisation of phospholipase A1 (Vespapase, Ves a 1) from Thai banded tiger wasp (Vespa affinis) venom.

The Thai banded tiger wasp (Vespa affinis) is one of the most dangerous vespid species in Southeast Asia, and stinging accidents involving this species still cause fatalities. In the present study, four forms of V. affinis phospholipase A(1) were identified through a proteomics approach.

Heteromtoxin (HmTx), a novel heterodimeric phospholipase A(2) from Heterometrus laoticus scorpion venom.

Heteromtoxin (HmTx) is a group III phospholipase A(2) produced in Heterometrus laoticus, in Thailand. In this study, HmTx was purified from venom by separation chromatography, and the PLA(2) activity of the fractions was determined by lecithin agar assay. The enzyme is an acidic protein with a pI of 5.