Portal de Periódicos da CAPES

Potent Anti-Calmodulin Activity of Cyclotetradepsipeptides Isolated from Isaria fumosorosea Using a Newly Designed Biosensor

2015; SAGE Publishing; Volume: 10; Issue: 1 Linguagem: Inglês

10.1177/1934578x1501000128

1934-578X

Abraham Madariaga‐Mazón, Martín González‐Andrade, Conchita Toriello, Hortensia Navarro-Barranco, Rachel Mata,

Neurobiology and Insect Physiology Research

Seven cyclotetradepsipeptides, namely beauverolides C (1), F (2), I (3), J a (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- AF 350 ; these peptides displayed high affinity to the protein with dissociation constants ( K d ) ranging from 0.078 μM to 3.44 μM. Beauverolide J a , 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.