Osmotin from Calotropis procera latex: New insights into structure and antifungal properties

This study aimed at investigating the structural properties and mechanisms of the antifungal action of CpOsm, a purified osmotin from Calotropis procera latex. Fluorescence and CD assays revealed that the CpOsm structure is highly stable, regardless of pH levels. Accordingly, CpOsm inhibited the spore germination of Fusarium solani in all pH ranges tested. The content of the secondary structure of CpOsm was estimated as follows: alpha-helix (20%), beta-sheet (33%), turned (19%) and unordered (28%). RMSD 1%. CpOsm was stable at up to 75 degrees C, and thermal denaturation (T(m)) was calculated to be 77.8 degrees C. This osmotin interacted with the negatively charged large unilamellar vesicles (LUVs) of 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-rac-1-glycerol (POPG), inducing vesicle permeabilization by the leakage of calcein. CpOsm induced the membrane permeabilization of spores and hyphae from Fusarium solani, allowing for propidium iodide uptake. These results show that CpOsm is a stable protein, and its antifungal activity involves membrane permeabilization, as property reported earlier for other osmotins and thaumatin-like proteins. (C) 2011 Elsevier B.V. All rights reserved.

On the release of metronidazole from natural rubber latex membranes

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

Latex use as an occlusive membrane for guided bone regeneration

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

Nitric oxide release using natural rubber latex as matrix

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

Evaluation of thermal behavior of latex membranes from genetically improved rubber tree (Hevea brasiliensis)

Thermal stability, thermal decomposition process, residual mass, temperature of glass transition (T-g) and temperature dependence of storage modulus (E'), were determined for latex membranes prepared from six clones of Hevea brasiliensis: IAC 331, IAC 332, IAC 333 and IAC 334 grown at experimental plantations of Instituto Agronomico de Campinas (IAC) in Votuporanga, São Paulo State, Brazil. Latex membranes from GT1 and RRIM 600 Asian matrix clones were used as references. The thermal behavior of latex membranes from genetically improved rubber trees was characterized using thermogravimetry/derivative thermogravimetry (TG/DTG), differential scanning calorimetry (DSC) and dynamic mechanical analysis (DMA). The thermal behavior of latex from clones studied in the present work showed similar features of the clones previously reported (IAC 40, IAC 300, IAC 301, IAC 328, IAC 329 and IAC 330), with mass loss in four consecutive steps, except IAC 333, which showed an additional mass loss step. (c) 2006 Elsevier B.V. All rights reserved.

Natural rubber latex used as drug delivery system in guided bone regeneration (GBR)

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

Metronidazole release using natural rubber latex as matrix

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

Comparative Study on the Technological Properties of Latex and Natural Rubber from Hancornia speciosa Gomes and Hevea brasiliensis

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

Purification of papain from fresh latex of Carica papaya

No presente trabalho apresenta-se um método de cristalização da papaína oriunda do látex fresco de mamão, o qual apresenta uma alta produtividade em relação aos métodos previamente descritos. A metodologia aqui descrita não envolve o uso de reagentes sulfidrílicos, a papaína foi obtida de forma praticamente pura, apresentando uma simples banda quando submetida a eletroforese, e com propriedades idênticas àquelas obtidas por outros métodos. A atividade específica foi determinada utilizando Z-gly-pNP e BAEE como substrato. A papaína obtida por essa metodologia, sem uso de substâncias tais como cisteína e ditiotreitol, apresenta-se na forma de um complexo com inibidores naturais, os quais podem ser removidos por diálise.

Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii

Miliin, a new thiol-dependent serine protease purified from the latex of Euphorbia milii possesses a molecular weight of 79 kDa, an isoelectric point of 4.3 and is optimally active at 60 degrees C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease.

Natural latex graft in lamellar and penetrating sclerectomies in rabbits

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)