Correlation Engine 2.0
Clear Search sequence regions

Sizes of these terms reflect their relevance to your search.

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. © 2020 The Authors. Chemical Biology & Drug Design published by John Wiley & Sons Ltd.


Kármen Szabó, Csaba Hámori, Gyöngyi Gyémánt. Gallotannins are non-specific inhibitors of α-amylase: Aggregates are the active species taking part in inhibition. Chemical biology & drug design. 2021 Feb;97(2):349-357

Expand section icon Mesh Tags

Expand section icon Substances

PMID: 32889761

View Full Text