Abstract
The family of benanomicin-pradimicin antibiotics (BPAs) is reviewed exhaustively with respect to its structural, functional, mechanistic and synthetic aspects. BPAs can be considered a unique class of compounds from the structural point of view due to the presence of a 5,6-dihydro-benzo[α]naphthacenequinone (DHBNQ) scaffold attached to a glycan moiety. The mechanism of action is ‘lectin-like’ and related to the selective recognition and binding to specific mannoside residues located at the surface of the membrane of fungal and viral pathogens. BPAs are prototype structures of non-peptidic small-size carbohydrate-binding agents (CBAs).
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