Madariaga-Mazón Abraham, González-Andradeb Martín, Toriello Conchita, Navarro-Barranco Hortensia, Mata Rachel
Nat Prod Commun. 2015 Jan;10(1):113-6.
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 μM to 3.44 μM. 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.
从昆虫病原真菌玫烟色棒束孢中分离出七种环四缩肽，即白僵菌素C（1）、F（2）、I（3）、Ja（4）、L（5）、M（6）和N（7）。使用新设计的钙调蛋白（CaM）生物传感器hCaM M124C-AF350评估白僵菌素作为潜在钙调蛋白抑制剂的活性；这些肽对该蛋白表现出高亲和力，解离常数（Kd）范围为0.078 μM至3.44 μM。结构中唯一含有色氨酸残基的白僵菌素Ja表现出最高亲和力。对接研究预测，白僵菌素可与钙调蛋白结合于与氯丙嗪（一种著名的钙调蛋白配体）相同的相互作用位点。
