Abstract:
:Human intestinal maltase (HMA) is an α-glucosidase that hydrolyses α-1,4-linkages from the non-reducing end of malto-oligosaccharides. HMA is an important target to discover of new drugs for the treatment of type 2 diabetes. In this study, 308,307 compounds were virtually screened with HMA using Autodock 3.0.5 in a WISDOM production environment to discover novel inhibitors. The 42 top-scoring free binding energy compounds, representing 17 groups containing potential hydrogen bonding with key residues in the active site pocket of HMA, were tested in vitro for their inhibitory activities against recombinant HMA expressed from Pichia pastoris. Compounds 17 and 18 were competitive inhibitors exclusively for HMA without any in vitro inhibition for human pancreatic α-amylase. The K(i) values were 20 μM for both compound 17 and 18.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Nguyen TT,Ryu HJ,Lee SH,Hwang S,Cha J,Breton V,Kim Ddoi
10.1007/s10529-011-0675-8subject
Has Abstractpub_date
2011-11-01 00:00:00pages
2185-91issue
11eissn
0141-5492issn
1573-6776journal_volume
33pub_type
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