6 documents found, page 1 of 1

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Mo-CBP3, an antifungal Chitin-Binding Protein from Moringa oleifera Seeds, is a...

Freire, José E. C.; Vasconcelos, Ilka M.; Moreno, Frederico B. M. B.; Batista, Adelina B.; Lobo, Marina D. P.; Pereira, Mirella L.; Lima, João P. M. S.

Mo-CBP3 is a chitin-binding protein from M. oleifera seeds that inhibits the germination and mycelial growth of phytopathogenic fungi. This protein is highly thermostable and resistant to pH changes, and therefore may be useful in the development of new antifungal drugs. However, the relationship of MoCBP3 with the known families of carbohydrate-binding domains has not been established. In the present study, fu...

Date: 2022   |   Origin: Oasisbr

Crystal structure of an antifungal osmotin-like protein from Calotropis procera...

Ramos, Márcio Viana; Oliveira, Raquel S. B. de; Pereira, Humberto M.; Moreno, Frederico B. M. B.; Lobo, Marina D. P.; Rebelo, Luciana Magalhães

CpOsm is an antifungal osmotin/thaumatin-like protein purified from the latex of Calotropis procera. The protein is relatively thermostable and retains its antifungal activity over a wide pH range; therefore, it may be useful in the development of new antifungal drugs or transgenic crops with enhanced resistance to phytopathogenic fungi. To gain further insight into the mechanism of action of CpOsm, its three-d...

Date: 2022   |   Origin: Oasisbr

A trypsin inhibitor purified from Cassia leiandra seeds has insecticidal activi...

Dias, Lucas P.; Oliveira, Jose T. A.; Rocha-Bezerra, Lady C. B.; Sousa, Daniele O. B.; Costa, Helen P. S.; Araújo, Nadine M. S.; Carvalho, Ana F. U.

A trypsin inhibitor from Cassia leiandra seeds, named ClTI, was purified, characterized, and its insecticidal activity against Aedes aegypti evaluated. ClTI was purified by DEAE-Cellulose and trypsin-Sepharose 4B chromatography, with a 15.5-fold purification and 2.4% yield. ClTI is composed of a 19,484 Da polypeptide chain as revealed by mass spectrometry, it is not a glycoprotein, its amino acid sequence is si...

Date: 2021   |   Origin: Oasisbr

Pattern of protein expression in the epididymis of Oligoryzomys nigripes (Crice...

Menezes, Tatiana Prata; Hill, Eric; Moura, Arlindo de Alencar; Lobo, Marina D. P.; Breton, Sylvie; Machado-Neves, Mariana

In the epididymis, epithelial cells work in a concerted manner to create a luminal environment for sperm maturation, transport, and storage. However, the cell functions may be affected by anthropogenic factors, causing negative impacts on male fertility. In our study, we describe the pattern of protein expression in the epithelium and luminal fluid from epididymis of Oligoryzomys nigripes, a South American sigm...

Date: 2018   |   Origin: Oasisbr

A chitin-binding protein purified from Moringa oleifera seeds presents anticand...

S. Neto, João X.; Pereira, Mirella L.; Oliveira, Jose T. A.; Bezerra, Lady C. B. Rocha; Lopes, Tiago D. P.; Costa, Helen P. S.; Sousa, Daniele O. B.

Candida species are opportunistic pathogens that infect immunocompromised and/or immunosuppressed patients, particularly in hospital facilities, that besides representing a significant threat to health increase the risk of mortality. Apart from echinocandins and triazoles, which are well tolerated, most of the antifungal drugs used for candidiasis treatment can cause side effects and lead to the development of ...

Date: 2017   |   Origin: Oasisbr

Antifungal activity of naphthoquinoidal compounds In vitro against fluconazole-...

Andrade Neto, João Batista de; Silva, Cecília R. da; Campos, Rosana S.; Siebra, Janaína T.; Silva, Rose A. C.; Gaspar, Danielle M.

In recent decades, the incidence of candidemia in tertiary hospitals worldwide has substantially increased. These infections are a major cause of morbidity and mortality; in addition, they prolong hospital stays and raise the costs associated with treatment. Studies have reported a significant increase in infections by non-albicans Candida species, especially C. tropicalis. The number of antifungal drugs on the...

Date: 2014   |   Origin: Oasisbr

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