English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

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. The sterol 14α-demethylase from  Trypanosoma cruzi  and  Leishmania infantum,  in particular, preferentially dock to taraxerol,  epi -oleanolic acid, and α/β-amyrim structural scaffolds. These structural information and predicted interactions can be exploited for fragment/structure-based antiprotozoal drug design.   Electronic supplementary material  The online version of this article (doi:10.1186/2193-1801-3-679) contains supplementary material, which is available to authorized users.

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