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001-es BibID:BIBFORM087586
Első szerző:Nagy-Szabó Kármen Annamária (vegyész)
Cím:Gallotannins are Non-Specific Inhibitors of α-Amylase: Aggregates are the Active Species taking part in Inhibition / Kármen Szabó, Csaba Hámori, Gyöngyi Gyémánt
Dátum:2021
ISSN:1747-0277
Megjegyzések:The versatile biological activity of gallotannins has been investigated for a long time, including their use as ?-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 ?-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 ?g/mL to 110 ?g/mL) and after enzyme-inhibitor pre-incubation (from 2.3 ?g/mL to 0.65 ?g/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 ?-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.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
gallotannin
inhibitor-promiscuity
aggregation
specificity
Megjelenés:Chemical Biology & Drug Design. - 97 : 2 (2021), p. 349-357. -
További szerzők:Hámori Csaba (1991-) (vegyész) Gyémánt Gyöngyi (1960-) (vegyész)
Pályázati támogatás:ÚNKP-19-3
Egyéb
Internet cím:DOI
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