19 research outputs found
Irrigation Scheduling in Crop Management System
Center pivor systems are widely used to suppress the irrigation needs of agricultural fields. In this article, we propose an autonomous to improve the low efficiency of this method of irrigation, developing a system based on the water requirement of the plantation, through field data (local temperature, local wind, soil moisture and precipitation forecast) and soil evapotranspiration calculation. The stored information will allow to calculatem the real evapotranspiration, not being necessary to restrict to lysometric measures. Accordingly, it is possible to schedule the irrigation for the period in which it has the lowest cost, considering the energy produced locally and the price of energy bought in the main market. Irrigation must be carried out within the time interval in which the plantation does not reach the wilding point, so it will be carried out at the time of the lowest cost.The present work was done and funded in the scope of the following project: Eco Rural IoT project funded by TETRAMAX-VALUECHAIN-TTX-1, and UID/EEA/00760/2019 funded by FEDER Funds through COMPETE program and by National Funds through FCT.info:eu-repo/semantics/publishedVersio
Identification of snake bradykinin-potentiating peptides (BPPs)-simile sequences in rat brain: potential BPP-like precursor protein?
Bradykinin-potentiating peptides (BPPs) from the South American pit viper snake venom were the first natural inhibitors of the human angiotensin I-converting enzyme (ACE) described. The pioneer characterization of the BPPs precursor from the snake venom glands by our group showed for the first time the presence of the C-type natriuretic peptide (CNP) in this same viper precursor protein. The confirmation of the BPP/CNP expression in snake brain regions correlated with neuroendocrine functions stimulated us to pursue the physiological correlates of these vasoactive peptides in mammals. Notably, several snake toxins were shown to have endogenous physiological correlates in mammals. In the present work, we expressed in bacteria the BPPs domain of the snake venom gland precursor protein, and this purified recombinant protein was used to raise specific polyclonal anti-BPPs antibodies. The correspondent single protein band immune-recognized in adult rat brain cytosol was isolated by 2DSDS/PAGE and/or HPLC, before characterization by MS fingerprint analysis, which identified this protein as superoxide dismutase (SOD, EC 1.15.1.1), a classically known enzyme with antioxidant activity and important roles in the blood pressure modulation. In silico analysis showed the exposition of the BPP-like peptide sequences on the surface of the 3D structure of rat SOD. These peptides were chemically synthesized to show the BPP-like biological activities in ex vivo and in vivo pharmacological bioassays. Taken together, our data suggest that SOD protein have the potential to be a source for putative BPP-like bioactive peptides, which once released may contribute to the blood pressure control in mammals
New formulation of an old drug in hypertension treatment: the sustained release of captopril from cyclodextrin nanoparticles
Mariangela de Burgos M de Azevedo1, Ljubica Tasic2, Juliana Fattori2, Fábio HS Rodrigues2, Fabiana C Cantos1, Leandro P Ribeiro1, Vanice de Paula3, Danielle Ianzer3, Robson AS Santos31Biopharmaceuticals and Hormones, Center of Biotechnology, Instituto de Pesquisas Energéticas e Nucleares (IPEN), Sao Paulo, Brazil; 2Chemical Biology Laboratory, Department of Organic Chemistry, Instituto de Química (UNICAMP), Sao Paulo, Brazil; 3Hypertension Laboratory, Department of Physiology and Biophysics, Instituto de Ciências Biológicas (ICB), Universidade Federal de Minas Gerais (ICB-UFMG), Minas Gerais, BrazilAbstract: Captopril (CAP) was the first angiotensin I-converting enzyme (ACE) inhibitor to be developed and is widely used in hypertension treatment. On the other hand, cyclodextrins (CDs) are cyclic oligosaccharides whose cone-shaped cavity allows formation of noncovalent inclusion complexes with appropriately sized guest molecules, thus modifying guest physical, chemical, and biological properties. Herein, the physicochemical characterization and in vivo ACE inhibition evaluation of seven CAP/CD complexes are reported. The inclusion complexes were prepared by spray-drying, freeze-drying, kneading, or lyophilization methods and characterized by nuclear magnetic resonance, Fourier-transformed infrared spectroscopy, X-ray diffraction, differential scanning calorimetry, and scanning electron microscopy techniques. In vivo assays compared CAP and CAP/CD complex administration (0.5 mg kg-1 or 0.09 mg kg-1, n = 4–7) to evaluate the ACE inhibition by continuous infusion of angiotensin I (30 ng 50 µL-1 min-1) in conscious Wistar rats. The physicochemical analysis demonstrated complete amorphization and complexation between CAP and CDs, indicating the substitution of water molecules inside the CD cavity with CAP. During the infusion of angiotensin I, the administration of all CAP/CD complexes induced a reduction in mean arterial pressure similar to that observed upon CAP administration. The nanoparticles obtained by the kneading method (CAP/α-CD:KM) showed a potent and long-lasting inhibitory activity (~22 hours) on the angiotensin I pressor effect. The results suggest that the inclusion complex of CAP and α-CD can function as a novel antihypertensive formulation that may improve therapeutic use of CAP by reducing its oral dose administration to once per day, thus providing better quality of life for almost 25% of the world's population who suffer from hypertension.Keywords: captopril, cyclodextrin nanoparticles, sustained releas
Tityus serrulatus Hypotensins: a new family of peptides from scorpion venom.
International audienceUsing a proteomic approach, a new structural family of peptides was put in evidence in the venom of the yellow scorpion Tityus serrulatus. Tityus serrulatus Hypotensins (TsHpt) are random-coiled linear peptides and have a similar bradykinin-potentiating peptide (BPP) amino acid signature. TsHpt-I (2.7kDa), the first member of this family, was able to potentiate the hypotensive effects of bradykinin (BK) in normotensive rats. Using the C-terminal of this peptide as a template, a synthetic analog peptide (TsHpt-I([17-25])) was designed to held the BK-potentiating effect. A relevant hypotensive effect, independent on BK, was also observed on both TsHpt (native and synthetic). To better evaluate this hypotensive effect, we examined the vasorelaxation of aortic rings from male Wistar rats and the peptides were able to induce endothelium-dependent vasorelaxation dependent on NO release. Both TsHpt could not inhibit ACE activity. These peptides appear to exert their anti-hypertensive effect through NO-dependent and ACE-independent mechanisms
Effects of CGEN-856S and losartan administration on the cardiomyocyte diameters of isoproterenol-treated rats.
<p>Animals were treated with isoproterenol (ISO) for 7 days to induce heart hypertrophy or with olive oil as a control. The effects of CGEN-856S were compared to those of saline as a negative control (Veh) or losartan (LOS) as a positive control. Values are expressed as mean ± standard error of the mean (SEM), nâ=â4â5 animals. *<i>P</i><0.05 vs. oil +Veh; <sup>#</sup><i>P</i><0.05 vs. ISO+Veh; <sup>α</sup><i>P</i><0.05 vs. ISO+LOS.</p
Effects of CGEN-856S and captopril administration on left ventricular infarct area.
<p>(A) Representative photomicrographs and (B) quantification of the infarct area of animals treated with CGEN-856S or captopril. Values are expressed as mean ± SEM, nâ=â7â8 animals. MI: myocardial infarction. *<i>P</i><0.05 vs. sham; <sup>#</sup><i>P</i><0.05 vs. MI+vehicle.</p
Effects of CGEN-856S and captopril administration on (A) systolic tension, (B) diastolic tension, (C) +dT/dt, (D) -dT/dt, (E) coronary flow, and (F) heart rate of rat hearts with myocardial infarction (MI).
<p>Values are expressed as mean ± SEM, nâ=â7â8 animals. *<i>P</i><0.05 vs. sham; <sup>#</sup><i>P</i><0.05 vs. MI+vehicle; <sup>α</sup><i>P</i><0.05 vs. MI+captopril.</p