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Keywords = Light subunit mushroom tyrosinase

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Article
In Silico Study to Develop a Lectin-Like Protein from Mushroom Agaricus bisporus for Pharmaceutical Application
by Wangsa Tirta ISMAYA, YUNITA, Sophi DAMAYANTI, Caroline WIJAYA, Raymond R. TJANDRAWINATA, Debbie Sofie RETNONINGRUM and Heni RACHMAWATI
Sci. Pharm. 2016, 84(1), 203-217; https://doi.org/10.3797/scipharm.ISP.2015.11 - 14 Feb 2016
Cited by 15 | Viewed by 4094
Abstract
A lectin-like protein of unknown function designated as LSMT was recently discovered in the edible mushroom Agaricus bisporus. The protein shares high structural similarity to HA-33 from Clostridium botulinum (HA33) and Ricin-B-like lectin from the mushroom Clitocybe nebularis (CNL), which have been [...] Read more.
A lectin-like protein of unknown function designated as LSMT was recently discovered in the edible mushroom Agaricus bisporus. The protein shares high structural similarity to HA-33 from Clostridium botulinum (HA33) and Ricin-B-like lectin from the mushroom Clitocybe nebularis (CNL), which have been developed as drug carrier and anti-cancer, respectively. These homologous proteins display the ability to penetrate the intestinal epithelial cell monolayer, and are beneficial for oral administration. As the characteristics of LSMT are unknown, a structural study in silico was performed to assess its potential pharmaceutical application. The study suggested potential binding to target ligands such as HA-33 and CNL although the nature, specificity, capacity, mode, and strength may differ. Further molecular docking experiments suggest that interactions between the LSMT and tested ligands may take place. This finding indicates the possible use of the LSMT protein, initiating new research on its use for pharmaceutical purposes. Full article
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