Peptides Inhibitors
Mostrando 1-12 de 287 artigos, teses e dissertações.
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1. N-Myristoyltransferases as antileishmanial targets: a piggyback approach with benzoheterocyclic analogues
Leishmaniasis is one of the neglected diseases that remain in need for pharmacological alternatives. In this context, N-Myristoyltransferases (NMT) arise as interesting targets to explore since they are involved in the co/post-translational processing of peptides which are responsible for host cell invasion. Studies that consider these enzymes as targets poi
Braz. J. Pharm. Sci.. Publicado em: 24/10/2019
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2. Subproteome of Lachesis muta rhombeata venom and preliminary studies on LmrSP-4, a novel snake venom serine proteinase
Abstract Background: Lachesis muta rhombeata is one of the venomous snakes of medical importance in Brazil whose envenoming is characterized by local and systemic effects which may produce even shock and death. Its venom is mainly comprised of serine and metalloproteinases, phospholipases A2 and bradykinin-potentiating peptides. Based on a previously report
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 15/04/2019
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3. Protease inhibitory, insecticidal and deterrent effects of the trypsin-inhibitor benzamidine on the velvetbean caterpillar in soybean
Abstract The recognition of protease inhibitors with insecticidal activity is important as a basis for the development of mimetic peptides with potential use as biorational insecticides. We sprayed benzamidine on soybean plants and assessed whether this potent synthetic trypsin-inhibitor has protease inhibitory, insecticidal and deterrent effects on the velv
An. Acad. Bras. Ciênc.. Publicado em: 18/10/2018
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4. Isolation and biochemical characterization of bradykinin-potentiating peptides from Bitis gabonica rhinoceros
Abstract Background: Venoms represent a still underexplored reservoir of bioactive components that might mitigate or cure diseases in conditions in which conventional therapy is ineffective. The bradykinin-potentiating peptides (BPPs) comprise a class of angiotensin-I converting enzyme (ACE) inhibitors. The BPPs usually consist of oligopeptides with 5 to 13
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 08/02/2018
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5. Highlights in the knowledge of brown spider toxins
Abstract Brown spiders are venomous arthropods that use their venom for predation and defense. In humans, bites of these animals provoke injuries including dermonecrosis with gravitational spread of lesions, hematological abnormalities and impaired renal function. The signs and symptoms observed following a brown spider bite are called loxoscelism. Brown spi
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 16/03/2017
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6. A spider derived peptide, PnPP-19, induces central antinociception mediated by opioid and cannabinoid systems
Abstract Background Some peptides purified from the venom of the spider Phoneutria nigriventer have been identified as potential sources of drugs for pain treatment. In this study, we characterized the antinociceptive effect of the peptide PnPP-19 on the central nervous system and investigated the possible involvement of opioid and cannabinoid systems in i
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 19/01/2017
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7. Angiotensin-converting enzyme inhibitors of Bothrops jararaca snake venom affect the structure of mice seminiferous epithelium
Background Considering the similarity between the testis-specific isoform of angiotensin-converting enzyme and the C-terminal catalytic domain of somatic ACE as well as the structural and functional variability of its natural inhibitors, known as bradykinin-potentiating peptides (BPPs), the effects of different synthetic peptides, BPP-10c (
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 29/09/2015
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8. Characterization of Leiurus abdullahbayrami (Scorpiones: Buthidae) venom: peptide profile, cytotoxicity and antimicrobial activity
Background Scorpion venoms are rich bioactive peptide libraries that offer promising molecules that may lead to the discovery and development of new drugs. Leiurus abdullahbayrami produces one of the most potent venoms among Turkish scorpions that provokes severe symptoms in envenomated victims. Methods In the present study, the peptide profile of the v
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 02/12/2014
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9. Proteases virais: importantes alvos terapêuticos de compostos peptideomiméticos
Proteases catalyze the hydrolysis of peptide bonds of proteins and peptides to produce smaller peptides and free amino acids. These enzymes are involved in physiologic processes such as blood coagulation and cellular death, and are related to life cycle of several viruses, such as hepatitis C, dengue, and AIDS. These features make most of proteases very impo
Quím. Nova. Publicado em: 2014-04
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10. Effects of hydrolysis and digestion in vitro on the activity of bovine plasma hydrolysates as inhibitors of the angiotensin I converting enzyme
The angiotensin I-converting enzyme (ACE) inhibiting activity of bovine plasma hydrolyzates obtained by Alcalase 2.4 L at different degrees of hydrolysis (DH) was evaluated. For the evaluation of ACE inhibition (ACEI), Hippuryl-His-Leu was used as substrate and the amount of hippuric acid liberated by non-inhibiting ACE was determined by spectrophotometry at
Braz. arch. biol. technol.. Publicado em: 31/01/2014
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11. A bradykinin-potentiating peptide (BPP-10c) from Bothrops jararaca induces changes in seminiferous tubules
Background The testis-specific isoform of angiotensin-converting enzyme (tACE) is exclusively expressed in germ cells during spermatogenesis. Although the exact role of tACE in male fertility is unknown, it clearly plays a critical function in spermatogenesis. The dipeptidase domain of tACE is identical to the C-terminal catalytic domain of somatic ACE (sAC
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 06/11/2013
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12. Purificação e caracterização biológica de uma nova serinoprotease com atividade trombina"like" do veneno total de Brothrops andianus (TLBan) / Purification and biological characterization of a new serine protease with thrombin "like" activity the whole venom of Brothrops andianus (TLBan)
In this word, a new serine protease with thrombin "like" activity the venom of Bothrops andianus (TLBan), snake of the Andes of Peru, was isolated by two steps: molecular exclusion chromatography G-75 and liquid chromatography in reversed-phase HPLC; with a high degree of purity and molecular homegenidade. Through of electrophoresis on SDS-PAGE shows the TLB
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 27/02/2012