Proteomic Characterization of the Hyaluronidase (EC 3.2.1.35) from the Venom of the Social Wasp Polybia paulista

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Monoamine oxidase inhibitory activities of indolylalkaloid toxins from the venom of the colonial spider Parawixia bistriata: Functional characterization of PwTX-I

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Biochemical and cytochemical studies of the enzymatic activity of the venom glands of workers of honey bee Apis mellifera L. (Hymenoptera, Apidae)

Biochemical studies revealed that the activity of some hydrolytic enzymes from the venom glands of honey bee Apis mellifera was higher in workers of 14 days of age than in those of 40 days. Among these enzymes, the highest activity was recorded for acid phosphatase, which was cytochemically detected throughout the length of the secretory filament and surrounding the canaliculi of the distal region of the reservoir. The acid phosphatase was considered to be a typical secretion product, since it was present in the cytoplasm as well as in the canaliculi of the secretory cells. (c) 2009 Elsevier Ltd. All rights reserved.

Profiling the peptidome of the venom from the social wasp Agelaia pallipes pallipes

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Histochemistry and Protein Profile of The Venom Glands of Workers of Neoponera villosa Ants (Hymenoptera: Ponerinae)

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Brown Recluse Spider Venom: Proteomic Analysis and Proposal of a Putative Mechanism of Action

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Polybioside, a Neuroactive Compound from the Venom of the Social Wasp Polybia paulista

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Proteomic characterization of the multiple forms of the PLAs from the venom of the social wasp Polybia paulista

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Profiling the Proteome of the Venom from the Social Wasp Polybia paulista: A Clue to Understand the Envenoming Mechanism

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Proteomic View of the Venom from the Fire Ant Solenopsis invicta Buren

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Structural and functional characterization of N-terminally blocked peptides isolated from the venom of the social wasp Polybia paulista

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Cytochemical studies of the nuclei of the venom glands' cells of Apis mellifera (Hymenoptera, Apidae)

Cytochemistry studies of the nuclei of the venom glands' cells of worker bees of Apis mellifera indicated that there is a higher activity in the young workers while there is a predominance of degenerative characteristics in the older workers. In addition, we demonstrated that there is an occurrence of differential nuclear synthetic activities between the cells of the distal and the proximal regions of the secretory filament and of the venom reservoir. Signs of a higher nuclear activity were evidenced at the distal regions of this gland in 14-day old workers, while at the more proximal regions of the venom gland of 40-day old workers we identified the most obvious signs of degeneration. Therefore, it was evident that the process of glandular degeneration begins at the distal region of the venom gland instead of beginning at the proximal region as had been established previously. In addition, characteristics of nuclear synthetic activities were noted in the cells of the proximal region of the reservoir; these cells were thought to be non-secretory.

How C-terminal carboxyamidation alters the biological activity of peptides from the venom of the eumenine solitary wasp

Inflammatory peptides display different types of post-transcriptional modifications, such as C-terminal amidation, that alter their biological activity. Here we describe the structural and molecular dynamics features of the mast cell degranulating peptide, eumenine mastoparan-AF (EMP-AF-NH2), found in the venom of the solitary wasp, and of its carboxyl-free C-terminal form (EMP-AF-COO-) characterized by a reduced activity. Circular dichroism indicates that both peptides switch from a random coil conformation in water to a helical structure in TFE and SDS micelles. NMR data, in 30% TFE, reveal that the two peptides fold into an alpha-helix spanning most of their length, while they differ in terms of molecular rigidity. To understand the origins of the conformational flexibility observed in the case of EMP-AF-COO-, a 5 ns MD simulation was carried out for each peptide, in an explicit water/TFE environment. The results show that the two peptides differ in an H-bond between Leu14 NH2 and the backbone carbonyl of Ile11. The loss of that H-bond in EMP-AF-COO- leads to a significant modification of its structural dynamics. In fact, as evidenced by essential dynamics analysis, while EMP-AF-NH2 exists mainly as a rigid structure, EMP-AF-COO- presents two helical stretches that fluctuate in some sort of independent fashion. We conclude that the diverse biological activity of the two peptides is not simply due to the reduction of the net positive charge, as generally suggested, but also to a structural perturbation of the amphipathic alpha-helix that affects their ability to perturb the cell membrane.

Effects of Spider Venom Toxin PWTX-I (6-Hydroxytrypargine) on the Central Nervous System of Rats

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)