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},
 identifiers = {[object Object]},
 volume = {10},
 id = {e9279949-f977-3b70-9631-afd8892afa5a},
 created = {2017-08-31T00:54:40.912Z},
 file_attached = {false},
 profile_id = {7da96f2b-cf05-3448-83f2-2c1e91a65514},
 last_modified = {2017-08-31T00:57:49.704Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 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}
}
Downloads: 0