RESUMEN
Several under-explored Aspergillus sp. produce intriguing heptapeptides containing a γ-aminobutyric acid (GABA) residue with as yet unknown biological functions. In this study, a new GABA-containing heptapeptide - unguisin J (1) - along with known unguisin B (2) were isolated from a solid culture of Aspergillus heteromorphus CBS 117.55. The structure of compound 1 was elucidated by extensive 1D and 2D NMR spectroscopic analysis including HSQC, HMBC, COSY, and 2D NOESY as well as HRESIMS. The stereochemistry of 1 and 2 was determined by Marfey's method. A biosynthetic gene cluster (BGC) encoding unguisins B and J was compared to characterized BGCs in other Aspergillus sp. Since the unguisin family of heptapetides incorporate different amino acid residues at different positions of the peptide, the A and C domains of the UngA NRPS were analyzed in an attempt to understand the lack of substrate specificity observed.
