Abstract:
:Alpha-glucosidase is considered to be an important target for the treatment of noninsulin-dependent diabetes. In this work, the inhibitory effects of polyoxometalates (POMs) affected by three different factors (heteroatom, transition metal substitution element and vanadium substitution number) on α-glucosidase were studied. We found that POMs with Keggin-type and vanadium-substituted Dawson-type structures act as effective and mostly competitive inhibitors for α-glucosidase (IC50 values around 40-160 μM), and most compounds can compete with the substrate for the active site of α-glucosidase. By analyzing and comparing the inhibitory effects of each series of POMs on α-glucosidase, the results demonstrated that the structure and composition of the POMs themselves may indirect influence on their inhibitory capabilities. Moreover, we gained initial information about the structure-inhibition relationship of different POMs. More intriguingly, molecular docking simulation suggested that all compounds bind into the active site of α-glucosidase by multiple van-der-Waals and hydrogen bond interactions. Our kinetic data demonstrate the considerable potential of POMs for the development of clinically valuable α-glucosidase inhibitors.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Chi G,Wang L,Chen B,Li J,Hu J,Liu S,Zhao M,Ding X,Li Ydoi
10.1016/j.jinorgbio.2019.110784subject
Has Abstractpub_date
2019-10-01 00:00:00pages
110784eissn
0162-0134issn
1873-3344pii
S0162-0134(19)30292-2journal_volume
199pub_type
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pub_type: 杂志文章,评审
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更新日期:2005-06-01 00:00:00