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Acaconin, a chitinase-like antifungal protein with cytotoxic and anti-HIV-1 reverse transcriptase activities from Acacia confusa seeds

100%

Lam S. K., Ng T. B.

Acta Biochimica Polonica

2010

tom 57

nr 3

From the seeds of Acacia confusa, a chitinase-like antifungal protein designated as acaconin that demonstrated antifungal activity toward Rhizoctonia solani with an IC50 of 30 ± 4 μM was isolated. Acaconin demonstrated an N-terminal sequence with pronounced similarity to chitinases and a molecular mass of 32 kDa. It was isolated by chromatography on Q-Sepharose, SP-Sepharose and Superdex 75 and was not bound by either ion exchanger. Acaconin was devoid of chitinase activity. The antifungal activity against Rhizoctonia solani was completely preserved from pH 4 to 10 and from 0ºC to 70ºC. Congo Red staining at the tips of R. solani hyphae indicated inhibition of fungal growth. However, there was no antifungal activity toward Mycosphaerella arachidicola, Fusarium oxysporum, Helminthosporium maydis, and Valsa mali. Acaconin inhibited proliferation of breast cancer MCF-7 cells with an IC50 of 128 ± 9 μM but did not affect hepatoma HepG2 cells. Its IC50 value toward HIV-1 reverse transcriptase was 10 ± 2.3 μM. The unique features of acaconin include relatively high stability when exposed to changes in ambient pH and temperature, specific antifungal and antitumor actions, potent HIV-reverse transcriptase inhibitory activity, and lack of binding by strongly cationic and anionic exchangers.

Novel galactonic acid-binding hexameric lectin from Hibiscus mutabilis seeds with antiproliferative and potent HIV-1 reverse transcriptase inhibitory activities

100%

Lam S. K., Ng T. B.

Acta Biochimica Polonica

2009

tom 56

nr 4

649-654

A hexameric 150-kDa lectin was isolated from dried Hibiscus mutabilis seeds using a chromatographic protocol that involved ion exchange chromatography on SP-Sepharose, and gel filtration on Superdex 75 and Superdex 200. The lectin was not adsorbed on SP-Sepharose and was eluted from the Superdex 75 column in the void volume. It was eluted in the first peak from Superdex 200. It was strongly adsorbed on DEAE-cellulose and Q-Sepharose and could not be easily desorbed. The hemagglutinating activity of the lectin, which was stable at pH 4-7 and up to 50oC, could be inhibited by 25 mM galactonic acid. This is the first report of a galactonic acid-binding lectin. It potently inhibited HIV-1 reverse transcriptase with an IC50 of 0.2 µM. It exhibited weak antiproliferative activity towards both hepatoma HepG2 cells (40% inhibition) and breast cancer MCF-7 cells (50% inhibition) at 100 µM concentration of the lectin. It did not inhibit mycelial growth of a number of fungi tested.

Ograniczanie wyników

2 Acta Biochimica Polonica

2 Lam S. K.

2 Ng T. B.

1 2010

1 2009

Wyniki wyszukiwania

Acaconin, a chitinase-like antifungal protein with cytotoxic and anti-HIV-1 reverse transcriptase activities from Acacia confusa seeds

Novel galactonic acid-binding hexameric lectin from Hibiscus mutabilis seeds with antiproliferative and potent HIV-1 reverse transcriptase inhibitory activities