Ipomoeassin F

Ipomoeassin F is a potent and selective endoplasmic reticulum (ER) protein-translocation inhibitor by targeting the pore-forming subunit of the Sec61 complex (Sec61α) at the ER membrane. Ipomoeassin F selectively inhibits the ER membrane translocation of SARS-CoV-2 proteins. Ipomoeassin F block the ER translocation of secretory proteins and type I transmembrane proteins (TMPs), but not type III TMPs[1][2][3].

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[1]Peristera Roboti, et al.Ipomoeassin-F disrupts multiple aspects of secretory protein biogenesis. Sci Rep. 2021 Jun 2;11(1):11562.|[2]Shugeng Cao, et al. Ipomoeassin F, a new cytotoxic macrocyclic glycoresin from the leaves of Ipomoea squamosa from the Suriname rainforest.Nat Prod Res. 2007 Aug;21(10):872-6.|[3]Sarah O'Keefe, et al. Ipomoeassin-F inhibits the in vitro biogenesis of the SARS-CoV-2 spike protein and its host cell membrane receptor. J Cell Sci. 2021 Feb 19;134(4):jcs257758.