Potent anti-calmodulin activity of cyclotetradepsipeptides isolated from Isaria fumosorosea using a newly designed biosensor
| Autor: | Rachel Mata, Hortensia Navarro-Barranco, Abraham Madariaga-Mazón, Conchita Toriello, Martín González-Andradeb |
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| Rok vydání: | 2015 |
| Předmět: |
Pharmacology
biology Calmodulin Chemistry Stereochemistry Tryptophan Plant Science General Medicine Biosensing Techniques biology.organism_classification Dissociation constant Hemiptera Complementary and alternative medicine Docking (molecular) Depsipeptides Drug Discovery Entomopathogenic fungus biology.protein Animals Beauverolides Paecilomyces Biosensor Isaria fumosorosea |
| Zdroj: | ResearcherID Scopus-Elsevier |
| ISSN: | 1934-578X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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