Unknown

Dataset Information

0

Discovery of a novel hybrid from finasteride and epristeride as 5?-reductase inhibitor.


ABSTRACT: Finasteride and epristeride both inhibit 5?-reductase with high potency via competitive and non-competitive mechanism, respectively. A new hybrid of finasteride and epristeride was designed as a new 5?-reductase inhibitor based on combination principles in medicinal chemistry. Human 5?-reductase was chosen as a plausible surrogate of 5?-reductase type II and the results indicate that although the hybrid compound possesses the main bulk of epristeride, its inhibitory mechanism is same as of finasteride. The hybrid turned out to be a potent 5?-reductase inhibitor in low IC(50) ranges.

SUBMITTER: Yao Z 

PROVIDER: S-EPMC7296779 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Discovery of a novel hybrid from finasteride and epristeride as 5α-reductase inhibitor.

Yao Zhiyi Z   Xu Yingjun Y   Zhang Minmin M   Jiang Sheng S   Nicklaus Marc C MC   Liao Chenzhong C  

Bioorganic & medicinal chemistry letters 20101028 1


Finasteride and epristeride both inhibit 5α-reductase with high potency via competitive and non-competitive mechanism, respectively. A new hybrid of finasteride and epristeride was designed as a new 5α-reductase inhibitor based on combination principles in medicinal chemistry. Human 5β-reductase was chosen as a plausible surrogate of 5α-reductase type II and the results indicate that although the hybrid compound possesses the main bulk of epristeride, its inhibitory mechanism is same as of finas  ...[more]

Similar Datasets

| S-EPMC8154553 | biostudies-literature
| S-EPMC2740403 | biostudies-literature
| S-EPMC8121512 | biostudies-literature
| S-EPMC4677828 | biostudies-literature
| S-EPMC7373137 | biostudies-literature
| S-EPMC7591894 | biostudies-literature
| S-EPMC4269219 | biostudies-literature
| S-EPMC4429719 | biostudies-literature
| S-EPMC6572442 | biostudies-literature
| S-EPMC5526468 | biostudies-literature