Potent anti-calmodulin activity of cyclotetradepsipeptides isolated from isaria fumosorosea using a newly designed biosensor. Madariaga-Mazon, A.; Gonzalez-Andrade, M.; Toriello, C.; Navarro-Barranco, H.; and Mata, R. Natural Product Communications, 2015. abstract bibtex Seven cyclotetradepsipeptides, namely beauverolides C (1), F (2), I (3), Ja (4), L (5), M (6), and N (7), were isolated from the entomopathogenic fungus Isaria fumosorosea. The beauverolides were evaluated as potential calmodulin (CaM) inhibitors using the newly designed CaM biosensor hCaM M124C-AF350; these peptides displayed high affinity to the protein with dissociation constants (Kd) ranging from 0.078 M to 3.44 M. Beauverolide Ja, the only one containing a tryptophan residue in its structure, showed the highest affinity. The docking study predicted that beauverolides could bind to CaM in the same site of interaction as chlorpromazine, a well-known calmodulin ligand.
@article{
title = {Potent anti-calmodulin activity of cyclotetradepsipeptides isolated from isaria fumosorosea using a newly designed biosensor},
type = {article},
year = {2015},
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abstract = {Seven cyclotetradepsipeptides, namely beauverolides C (1), F (2), I (3), Ja (4), L (5), M (6), and N (7), were isolated from the entomopathogenic fungus Isaria fumosorosea. The beauverolides were evaluated as potential calmodulin (CaM) inhibitors using the newly designed CaM biosensor hCaM M124C-AF350; these peptides displayed high affinity to the protein with dissociation constants (Kd) ranging from 0.078 M to 3.44 M. Beauverolide Ja, the only one containing a tryptophan residue in its structure, showed the highest affinity. The docking study predicted that beauverolides could bind to CaM in the same site of interaction as chlorpromazine, a well-known calmodulin ligand.},
bibtype = {article},
author = {Madariaga-Mazon, A. and Gonzalez-Andrade, M. and Toriello, C. and Navarro-Barranco, H. and Mata, R.},
journal = {Natural Product Communications},
number = {1}
}