Unknown

Dataset Information

0

Interactions of antiparasitic sterols with sterol 14?-demethylase (CYP51) of human pathogens.


ABSTRACT: Sterol 14?-demethylase is a validated and an attractive drug target in human protozoan parasites. Pharmacological inactivation of this important enzyme has proven very effective against fungal infections, and it is a target that is being exploited for new antitrypanosomal and antileishmanial chemotherapy. We have used in silico calculations to identify previously reported antiparasitic sterol-like compounds and their structural congeners that have preferential and high docking affinity for CYP51. The sterol 14?-demethylase from Trypanosoma cruzi and Leishmania infantum, in particular, preferentially dock to taraxerol, epi-oleanolic acid, and ?/?-amyrim structural scaffolds. These structural information and predicted interactions can be exploited for fragment/structure-based antiprotozoal drug design.

SUBMITTER: Warfield J 

PROVIDER: S-EPMC4410773 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

altmetric image

Publications

Interactions of antiparasitic sterols with sterol 14α-demethylase (CYP51) of human pathogens.

Warfield Jasmine J   Setzer William N WN   Ogungbe Ifedayo Victor IV  

SpringerPlus 20141120


Sterol 14α-demethylase is a validated and an attractive drug target in human protozoan parasites. Pharmacological inactivation of this important enzyme has proven very effective against fungal infections, and it is a target that is being exploited for new antitrypanosomal and antileishmanial chemotherapy. We have used in silico calculations to identify previously reported antiparasitic sterol-like compounds and their structural congeners that have preferential and high docking affinity for CYP51  ...[more]

Similar Datasets

| S-EPMC3488290 | biostudies-literature
| S-EPMC3269163 | biostudies-literature
| S-EPMC4505289 | biostudies-literature
| S-EPMC4904373 | biostudies-literature
| S-EPMC3591892 | biostudies-literature
| S-EPMC6881533 | biostudies-literature
| S-EPMC7496091 | biostudies-literature
| S-EPMC7822023 | biostudies-literature
| S-EPMC4178690 | biostudies-literature
| S-EPMC3391166 | biostudies-literature