Abstract
Fungal immunomodulatory proteins (FIPs), a group of small proteins with notable immunomodulatory activity, have been investigated for their use as a natural food-derived potential anti-tumor drug. However, anti-tumor activity is always confined by the compounds’ stability during various processing stages. In this study, the correlation between thermal stability and structural features has been evaluated. FIP-nha from Nectria haematococca, recombinantly expressed in E.coli, showed significant anti-tumor activity and considerable thermostability. The melting temperature of rFIP-nha was higher than that of rFIP-gmi, rFIP-fve, and rLZ-8. Structure studies indicated that rFIP-nha adopted a tetrameric structure and had a larger interface area, more intermolecular bonds and hydrophobic interaction than rFIP-gmi, rFIP-fve and rLZ-8. Molecular dynamic stimulation and biochemical studies further suggested that the tetramer formation correlated with the high thermostability of rFIP-nha. Structural insights into the thermostability of FIP-nha are valuable for comprehensive understanding the regulation mechanism of FIPs, and may help to enlarge their utilization.
| Original language | English |
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| Publication status | Published - 2021 |
| Event | 20th National Symposium on Agricultural Biochemistry and Molecular Biology - Mianyang, China Duration: 5 Aug 2021 → 9 Aug 2021 |
Conference
| Conference | 20th National Symposium on Agricultural Biochemistry and Molecular Biology |
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| Country/Territory | China |
| City | Mianyang |
| Period | 5/08/21 → 9/08/21 |