| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5159998 | Journal of Molecular Structure | 2017 | 25 Pages |
Abstract
The isolated crystal structure of 2 is in an excellent agreement with the computation in respect of the most stable tautomer. Combined single X-ray/molecular modeling studies including HYdrogen-DEsolvation (HYDE) analysis provided not only insights into the enzyme-inhibitor interaction within the binding site of the human MAO-B isoform, but also a valuable information regarding the most stable 1H-indazole tautomeric form of NTZ-1006 that contributes to its high potency against hMAO-B enzyme (IC50 0.586Â nm) and selectivity (>17000-fold) over the hMAO-A isoenzyme.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Nikolay T. Tzvetkov, Hans-Georg Stammler, Liudmil Antonov,