RESUMO Campomanesia adamantium é muito utilizada na medicina popular no tratamento de hipertensão, reumatismo e diabetes. Objetivou-se com o presente trabalho avaliar o rendimento, a composição química, e as atividades antimicrobiana e antioxidante do óleo essencial de folhas de C. adamantium submetidas a diferentes métodos e tempos de secagem. O delineamento utilizado foi inteiramente casualizado, com oito tratamentos e três repetições. O óleo essencial foi extraído por hidrodestilação das folhas e analisado por CG-EM. O tipo de secagem das folhas de C. adamantium influenciou no teor e na composição química do óleo essencial. Os constituintes espatulenol, óxido cariofileno e germacreno-B apresentaram maior concentração na maioria das procedências avaliadas. O óleo essencial das folhas de C. adamantium apresentou moderada atividade antibacteriana em relação a todos os micro-organismos testados. A atividade antioxidante se deu empregando-se o método de redução do radical estável DPPH, sendo observada fraca atividade antioxidante por meio do ensaio utilizado.

ABSTRACT C. adamantiumis widely used in popular medicine for thetreatment of hypertension, rheumatism and diabetes. This study looked to evaluate the essential oil yield, the chemical composition and the antimicrobial and antioxidant activities of the essential oil from leaves of C. adamantium. A completely randomized design was used with eight treatments and three replications. The essential oil obtained by hydrodestillation of the leaves was analyzed by GC-MS. The results show that the drying type and the processing of the leaf influence the content and chemical composition of the essential oil. The compounds spathulenol, caryophyllene oxide and germacrene-B have higher concentrationsin mostorigins. The essentialoil from theleaves of C.adamantiumshowed moderate bacterial activityagainst all tested microorganisms. The antioxidant activity was determined by the methods of reduction of the DPPH stable radical. The antioxidant activity was weak in the test used.

RESUMO O objetivo deste estudo foi avaliar o efeito antibacteriano e tripanocida in vitro do extrato hidroalcóolico das raízes de Tradescantia sillamontana Matuda (Commelinaceae), conhecida popularmente como veludo branco. Foi avaliada a atividade antibacteriana in vitro frente às bactérias Streptococcus mitis (CIM = 100 µg/mL; CMB = 150 µg/mL), Streptococcus mutans (CIM = 200 µg/mL; CMB = 220 µg/mL), Streptococcus sanguinis (CIM = 400 µg/mL; CMB = 425 µg/mL), Streptococcus sobrinus (CIM = 400 µg/mL; CMB = 420 µg/mL) e Bacteroides fragilis (CIM = 400 µg/mL; CMB = 430 µg/mL) pelo método de diluição em caldo. Os protozoários da família tripanossomatídeo causam doenças tropicais que costumam ser negligenciadas que costumam ser como a tripanossomíase, para a qual estão disponíveis poucos medicamentos. Neste contexto, o extrato hidroalcóolico das raízes de T. sillamontana também foi avaliado frente às formas tripomastigotas da cepa Y de Trypanosoma cruzi, com promissora atividade frente a este protozoário (IC50 = 2,4 µg/mL). Quando avaliada a atividade citotóxica frente a fibroblastos da linhagem LLCMK2, o extrato apresentou moderada citotoxicidade (CC50 = 480,37 µg/mL). Os resultados ora apresentados para o extrato hidroalcóolico das raízes de Tradescantia sillamontana Matuda demonstraram promissoras atividades antibacteriana e tripanocida, sendo uma fonte alternativa de produtos naturais com atividades contra T. cruzi e algumas bactérias do gênero Streptococcus e Bacteroides.

ABSTRACT The aim of this study was to investigate the in vitro, antibacterial and trypanocidal effect of the hydroalcoholic extract from the roots of Tradescantia sillamontana Matuda (Commelinaceae), commonly known as Veludo branco. The in vitro antibacterial activity against the standard bacteria Streptococcus mitis (MIC = 100µg/mL; MBC = 150 µg/mL), Streptococcus mutans (MIC = 200µg/mL; MBC = 220 µg/mL), Streptococcus sanguinis (MIC = 400µg/mL; MBC = 425 µg/mL), Streptococcus sobrinus (MIC = 400µg/mL; MBC = 420 µg/mL) andBacteroides fragilis (MIC = 400µg/mL; MBC = 430 µg/mL), using microdilution broth methods. Protozoans from the trypanosomatid family cause neglected tropical diseases such as trypanosomiasis, for which few drugs are available. In this context, the hydroalcoholic extract of the Tradescantia sillamontana roots was also investigated with regards to the in vitro effects against the trypomastigote forms of theY strain of Trypanosoma cruzi, showing strong activity against this parasite (IC50 = 2.4 µg/mL). When performing cytotoxic activity against fibroblasts LLCMK2 line, the extract showed moderate cytotoxicity (CC50 = 480.37 mg/mL). The results presented for the hydroalcoholic extract of the roots of Tradescantia sillamontana Matuda demonstrated effective antibacterial and trypanocidal activities and were shown to be an alternative source of natural products with activity against T. cruzi and some bacteria of the genus Streptococcus and Bacteroides.

O estímulo mecânico sabidamente provoca deformação de proteínas da matriz extracelular e da célula óssea, as quais se tornam ativas e sinalizam reações intracelulares que determinam o aumento da massa óssea. Estudos apontam a quinase de adesão focal (FAK) como uma proteína fundamental na sinalização da deformação celular causada pelo estímulo mecânico no osso, mas há necessidade de estudos in vivo que comprovem esse papel. Objetivos - Com o ultra-som de baixa potência, investigar a influência do estímulo mecânico na expressão da FAK no osso, e a possibilidade de detectar proteínas envolvidas com a proliferação celular óssea e muscular esquelética. Material e Métodos - Tíbias e fíbulas de ratos foram estimuladas com ultra-som de baixa potência durante 20 min/uma vez ao dia, por períodos de 7, 14 e 21 dias. O grupo controle não foi estimulado. Cada grupo continha 7 ratos. Quinze horas após o último estímulo, a tíbia e a fíbula foram retiradas para realização de immunoblotting, utilizando anticorpos específicos para identificar FAK, FAK-Tyr(P)-397, extracellular signal-regulated kinase-2 (ERK-2), ERK-1/2-Tyr(P)-204, insulin receptor substrate-1 (IRS-1) e IRS-2. O músculo esquelético da região estimulada foi extraído e submetido ao mesmo procedimento. Resultados - Analisando-se os resultados de immunoblotting comparativamente com o grupo controle, não foram detectadas FAK e FAK-Tyr(P)-397 no tecido ósseo, enquanto ERK-2, ERK-1/2-Tyr(P)-204, IRS-1 e IRS-2 foram identificados. No músculo esquelético, todas as proteínas estudadas foram identificadas, exceto IRS-2. Discussão e Conclusão: Os resultados sugerem que não deve haver quantidade suficiente de FAK no osso detectável pelo método utilizado. Por outro lado, observou-se que ERK-2, IRS-1 e IRS-2 são detectáveis no osso e devem responder ao estímulo mecânico. Além disso, o encontro dessas proteínas no tecido muscular abre novas perspectivas no estudo da influência das partes moles no processo de reparação do tecido ósseo.

It’s widely known that mechanical deformation of bone promotes activation of some proteins in the extracellular matrix and bone cells. These proteins are responsible for signaling intracellular reactions that determine bone mass growth. Studies indicate focal adhesion kinase (FAK) as a crucial protein to signal mechanical deformation caused by mechanical loading on bone, but evidences in vivo are required to prove this role. Objectives - Using a low-intensity ultrasound, investigate the influence of the mechanical loading on the expression of FAK in bone, and the possibility of detecting proteins involved on cellular proliferation of bone and skeletal muscle. Material and methods - Tibiae and fibulae of 12-weeks-rats were stimulated by low-intensity ultrasound during 20 minutes/once a day for periods of 7, 14 and 21 days. There were 4 groups, each one containing 7 rats. The control group was not stimulated. Fifteen hours after the last stimulation, the tibia and fibula were extracted for immunoblotting procedures with specific antibodies in order to evaluate FAK, FAK-Tyr(P)-397, extracellular signal-regulated kinase-2 (ERK-2), ERK-1/2-Tyr(P)-204, insulin receptor substrate-1 (IRS-1) and IRS-2. The skeletal muscle of the stimulated area was subjected to the same procedures. Results - Comparing the results of the different groups, both FAK and FAK-Tyr(P)-397 were not detected in bone. However, ERK-2, ERK-1/2-Tyr(P)-204, IRS-1 and IRS-2 were identified. Moreover, all the proteins studied were detected in skeletal muscle except for IRS-2. Discussion and conclusion - The results suggest there are no significant quantities of FAK in bone detectable by the methods used. In other hand, it was noted that ERK-2, ERK-1/2-Tyr(P)-204, IRS-1 and IRS-2 are detectable in bone and may be responsive to mechanical stimulation. In addition, the detection of these proteins in skeletal muscle, including FAK, opens up new perspectives on the study of the influence of this tissue on bone repair.

Serine-proteases are involved in vital processes in virtually all species. They are important targets for researchers studying the relationships between protein structure and activity, for the rational design of new pharmaceuticals. Trypsin was used as a model to assess a possible differential contribution of hydration water to the binding of two synthetic inhibitors. Thermodynamic parameters for the association of bovine ß-trypsin (homogeneous material, observed 23,294.4 ± 0.2 Da, theoretical 23,292.5 Da) with the inhibitors benzamidine and berenil at pH 8.0, 25ºC and with 25 mM CaCl2, were determined using isothermal titration calorimetry and the osmotic stress method. The association constant for berenil was about 12 times higher compared to the one for benzamidine (binding constants are K = 596,599 ± 25,057 and 49,513 ± 2,732 M-1, respectively; the number of binding sites is the same for both ligands, N = 0.99 ± 0.05). Apparently the driving force responsible for this large difference of affinity is not due to hydrophobic interactions because the variation in heat capacity (DCp), a characteristic signature of these interactions, was similar in both systems tested (-464.7 ± 23.9 and -477.1 ± 86.8 J K-1 mol-1 for berenil and benzamidine, respectively). The results also indicated that the enzyme has a net gain of about 21 water molecules regardless of the inhibitor tested. It was shown that the difference in affinity could be due to a larger number of interactions between berenil and the enzyme based on computational modeling. The data support the view that pharmaceuticals derived from benzamidine that enable hydrogen bond formation outside the catalytic binding pocket of ß-trypsin may result in more effective inhibitors.