{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9(1)"],"submitter":["Wang Y"],"pubmed_abstract":["Fungal immunoregulatory proteins (FIP) are effective small molecule proteins with broad-spectrum immunomodulatory and anti-cancer activities and can be potential agents for the development of clinical drugs and health food additives. In this study, a new member of FIP named FIP-bbo was obtained through Botryobasidium botryosum genome mining. FIP-bbo has the typical characteristics of FIP but is genetically distant from other FIPs. Recombinant FIP-bbo (rFIP-bbo) was produced in an optimized E. coli expression system, and the pure protein was isolated using a Ni-NTA column. Antineoplastic experiments suggested that FIP-bbo is similar to LZ-8 in inhibiting various cancer cells (Hela, Spac-1, and A549) at lower concentrations, but it is not as potent as LZ-8. The molecular mechanism by which F"],"journal":["Scientific reports"],"pagination":["5818"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6456589"],"repository":["biostudies-literature"],"pubmed_title":["Identification of a Novel Anti-cancer Protein, FIP-bbo, from Botryobasidium botryosum and Protein Structure Analysis using Molecular Dynamic Simulation."],"pmcid":["PMC6456589"],"pubmed_authors":["Gao YN","Bai R","Bao DP","Shang JJ","Chen HY","Wang Y","Wu YY"],"additional_accession":[]},"is_claimable":false,"name":"Identification of a Novel Anti-cancer Protein, FIP-bbo, from Botryobasidium botryosum and Protein Structure Analysis using Molecular Dynamic Simulation.","description":"Fungal immunoregulatory proteins (FIP) are effective small molecule proteins with broad-spectrum immunomodulatory and anti-cancer activities and can be potential agents for the development of clinical drugs and health food additives. In this study, a new member of FIP named FIP-bbo was obtained through Botryobasidium botryosum genome mining. FIP-bbo has the typical characteristics of FIP but is genetically distant from other FIPs. Recombinant FIP-bbo (rFIP-bbo) was produced in an optimized E. coli expression system, and the pure protein was isolated using a Ni-NTA column. Antineoplastic experiments suggested that FIP-bbo is similar to LZ-8 in inhibiting various cancer cells (Hela, Spac-1, and A549) at lower concentrations, but it is not as potent as LZ-8. The molecular mechanism by which F","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Apr","modification":"2026-04-29T16:00:31.892Z","creation":"2019-06-06T21:09:37Z"},"accession":"S-EPMC6456589","cross_references":{"pubmed":["30967569"],"doi":["10.1038/s41598-019-42104-1"]}}