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Screening An alpha-glucosidase Inhibitor from A Phage-displayed Peptide Library
1Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China. kyw0717@sunm.shcnc.ac.cn
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao Acta Biochimica Et Biophysica Sinica
|June 1, 2002
Abstract:
A phage-displayed peptide library was biopanned with Aspergillus niger glucoamylase. Three specifically binding phage clones (GB-1, GB-2 and GB-3) were identified after three cycles of screening and amplification. All three peptides contained a disulfide bridge, and the impairment of disulfide bond greatly lowered the binding activity. One peptide, cyclic KCHFEECLAY, representing the N-terminal 10 amino acid residues from GB-1, competitively inhibited A. niger glucoamylase (K(I) 0.2 mmol/L) as well as rat intestinal alpha-glucosidase (KI 1.4 mmol/L).