| Revista: | Brazilian Journal of Pharmaceutical Sciences |
| Base de datos: | PERIÓDICA |
| Número de sistema: | 000451948 |
| ISSN: | 1984-8250 |
| Autores: | Rasti, Behnam1 |
| Instituciones: | 1Islamic Azad University, Faculty of Basic Sciences, Lahijan, Guilan. Irán |
| Año: | 2022 |
| Volumen: | 58 |
| País: | Brasil |
| Idioma: | Inglés |
| Tipo de documento: | Artículo |
| Enfoque: | Experimental, aplicado |
| Resumen en inglés | Due to the fact that different isoforms of carbonic anhydrase play distinct physiological roles, their diseases/disorders involvement are different as well. Involvement in major disorders such as glaucoma, epilepsy, Alzheimer’s disease, obesity and cancers, have turned carbonic anhydrase into a popular case study in the field of rational drug design. Since carbonic anhydrases are highly similar with regard to their structures, selective inhibition of different isoforms has been a significant challenge. By applying a proteochemometrics approach, herein the chemical interaction space governed by acyl selenoureido benzensulfonamides and human carbonic anhydrases is explored. To assess the validity, robustness and predictivity power of the proteochemometrics model, a diverse set of validation methods was used. The final model is shown to provide valuable structural information that can be considered for new selective inhibitors design. Using the supplied information and to show the applicability of the constructed model, new compounds were designed. Monitoring of selectivity ratios of new designs shows very promising results with regard to their selectivity for a specific isoform of carbonic anhydrase |
| Disciplinas: | Química |
| Palabras clave: | Bioquímica, Anhidrasa carbónica, Modelación proteoquemométrica, Selectividad, Isoformas |
| Keyword: | Biochemistry, Carbonic anhydrase, Proteochemometric modeling, Selectivity, Isoforms |
| Texto completo: | Texto completo (Ver HTML) Texto completo (Ver PDF) |
