Gallotannins are non-specific inhibitors of α-amylase: Aggregates are the active species taking part in inhibition.
Chem Biol Drug Des
; 97(2): 349-357, 2021 02.
Article
en En
| MEDLINE
| ID: mdl-32889761
The versatile biological activity of gallotannins has been investigated for a long time, including their use as α-amylase inhibitors for the treatment of diabetes and its complications. The effectiveness of gallotannins on a wide range of enzymes refers to promiscuity. We proved that gallotannins are non-specific promiscuous α-amylase inhibitors, which exert their effect through their aggregates. A gallotannin of Aleppo oak origin fulfilled all the criteria for aggregators; significant changes could be observed in the IC50 values in the presence of Triton™ X-100 detergent (from 2.3 to 110 µg/ml) and after enzyme-inhibitor preincubation (from 2.3 to 0.65 µg/ml). Increasing the enzyme concentration also led to the moderation of the inhibition by gallotannin. In addition, we observed that gallotannin molecules are those, which are involved in aggregation, and discrete protein molecules are adsorbed to the aggregates. This was revealed by the increasing particle size of gallotannin, which became three orders of magnitude higher after 150 min, whereas the size of α-amylase remained unchanged. Consequently, gallotannins should be used as anti-diabetic drugs only if the necessity of higher dose due to their promiscuity is taken into account. Aggregation propensity should not be ignored in case of in vivo applications.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Taninos Hidrolizables
/
Inhibidores Enzimáticos
/
Alfa-Amilasas
Idioma:
En
Revista:
Chem Biol Drug Des
Asunto de la revista:
BIOQUIMICA
/
FARMACIA
/
FARMACOLOGIA
Año:
2021
Tipo del documento:
Article
País de afiliación:
Hungria
Pais de publicación:
Reino Unido