Seed germination and triterpenoid content of Anemopaegma arvense (Vell.) Stellfeld varieties.

Anemopaegma arvense (Vell.) Stellfeld, Bignoniaceae, is a native species of the Brazilian savanna (Cerrado) and is commonly known as catuaba among the local farmers. Seeds of three varieties were collected in different localities and submitted to germination and storage studies in attempting to domesticate this species as a medicinal crop for small farmers located in Brazilian Cerrado. Germination tests revealed that catuaba seeds presented a dormancy period of 6 weeks, and 63% of the seedlings have emerged after 12 weeks of the planting time. Storing catuaba seeds at low temperatures (?20 and ?196C) has not affected emergence and survival. These findings suggested that A. arvense seeds have an orthodox behavior resisting well to dehydration and low temperature storage. Three catuaba varieties were characterized morphologically and chemically. The presence of triterpenes such as oleanolic acid and betulinic acid were identified and quantified in these varieties. Previous report has shown that these compounds have promising anticancer activities and herein the results point that the aerial parts yielded more triterpenes than the roots. The combination of higher capacity and preferential accumulation of triterpenes in the aerial parts of catuaba makes this plant a potential candidate for agricultural production or in situ sustainable harvests as a promising alternative to the destructive collection of the natural population

Meeting the stakeholder needs and sustaining business through sustainability risk management practices: A case study of Malaysian environmentally sensitive companies

Sustainability issues such as climate change, carbon emissions, and energy consumption have become increasingly important issues among business organisations, academics and policy makers. Considering this complexity, stakeholders currently demanding companies to have a sound risk management that are aligned to their interest. Sustaining business requires a strong foundational on the economic, environmental and social aspects to address risks and capture value. Sustainability risk management (SRM) is a process that systematically integrates environmental, social, and economic aspects to address emerging risks and other non-quantifiable risk for company survival. This study aims to examine the impact of SRM practices on the company survival among the environmentally sensitive companies in Malaysia. A case study was carried out to examine the SRM implementation among the environmentally sensitive companies. The finding shows that leadership and compliance are considered as important factors in implementing SRM programme. Other factors such as sound risk culture, adequate risk management tools, and effective business continuity planning are crucial to support SRM implementation. Overall findings revealthat the companies are at the early stage implementing SRM programme and denote there is much room for improvement in the risk management process to create long-term value creation for the stakeholders. This study provides empirical evidence on the significance of SRM factors to the company survival. Given the huge environmental and social costs arising from sustainability issues, companies should intensify their effort to fully implement SRM programme across the organisation to sustain longer

Crystallization and preliminary X-ray diffraction analysis of a myotoxic Lys49-PLA2 from Bothrops jararacussu venom complexed with p-bromophenacyl bromide

A non-catalytic and myotoxic Lys49-PLA2 from B. jararacussu venom was crystallized with BPB inhibitor and X-ray diffraction data were collected. Preliminary analysis indicates that the ligand is bound to the His48 residue. Structure determination may provide insights into the myotoxic and cytotoxic mechanisms of Lys49-PLA2s

Bothrops moojeni myotoxin-II, a Lys49-phospholipase A(2) homologue: An example of function versatility of snake venom proteins

MjTX-II, a myotoxic phospholipase A(2) (PLA(2)) homologue from Bothrops moojeni venom, was functionally and structurally characterized. The MjTX-II characterization included: (i) functional characterization (antitumoral, antimicrobial and antiparasitic effects); (ii) effects of structural modifications by 4-bromophenacyl bromide (BPB), cyanogen bromide (CNBr), acetic anhydride and 2-nitrobenzenesulphonyl fluoride (NBSF); (iii) enzymatic characterization: inhibition by low molecular weight heparin and EDTA; and (iv) molecular characterization: cDNA sequence and molecular structure prediction. The results demonstrated that MjTX-II displayed antimicrobial activity by growth inhibition against Escherichia coli and Candida albicans, antitumoral activity against Erlich ascitic tumor (EAT), human breast adenocarcinoma (SK-BR-3) and human T leukemia cells (JURKAT) and antiparasitic effects against Schistosoma mansoni and Leishmania spp., which makes MjTX-II a promising molecular model for future therapeutic applications, as well as other multifunctional homologous Lys49-PLA(2)S or even derived peptides. This work provides useful insights into the structural determinants of the action of Lys49-PLA2 homologues and, together with additional strategies, supports the concept of the presence of others bioactive sites distinct from the catalytic site in snake venom myotoxic PLA(2)s. (c) 2005 Elsevier B.V. All rights reserved

Molecular characterization and phylogenetic analysis of JussuMP-I: A RGD-P-III class hemorrhagic metalloprotease from Bothrops jararacussu snake venom

Snake venom metalloproteases (SVMPs) embody zinc-dependent multidomain enzymes responsible for a relevant pathophysiology in envenomation. including local and systemic hemorrhage. The molecular features responsible for hemorrhagic potency of SVMPs have been associated with their multidomains structures which can target these proteins them to several receptors of different tissues and cellular types. BjussuMP-I. a SVMP isolated from the Bothrops jararacussu venom, has been characterized as a P-III hemorrhagic metalloprotease. The complete cDNA sequence of BjussuMP-I with 1641bp encodes open reading frames of 547 amino acid residues, which conserve the common domains of P-III high molecular weight hemorrhagic metalloproteases: (i) pre-pro-peptide, (ii) metalloprotease, (iii) disintegrin-like and (iv) rich cysteine domain. BjussuMP-I induced lyses in fibrin clots and inhibited collagen- and ADP-induced platelet aggregation. We are reporting, for the first time, the primary structure of an RGD-P-III class snake venom metalloprotease. A phylogenetic analysis of the BjussuMP-1 metalloprotease/catalytic domain was performed to get new insights into the molecular evolution of the metalloproteases. A theoretical molecular model of this domain was built through folding recognition (threading) techniques and refined by molecular dynamics simulation. Then, the final BjussuMP-I catalytic domain model was compared to other SVMPs and Reprolysin family proteins in order to identify eventual structural differences, which could help to understand the biochemical activities of these enzymes. The presence of large hydrophobic areas and some conserved surface charge-positive residues were identified as important features of the SVMPs and other metalloproteases. (C) 2006 Elsevier B.V. All rights reserved