Screening of peptide inhibitors of acetylcholinesterase from 12-mer random phage display peptide library.
- Author:
Xing-mei ZHANG
1
;
Yu-sheng SHI
;
Chun-xia WANG
Author Information
- Publication Type:Journal Article
- MeSH: Acetylcholinesterase; metabolism; Cholinesterase Inhibitors; metabolism; pharmacology; Humans; Peptide Library; Peptides; metabolism; pharmacology; Protein Binding
- From: Journal of Southern Medical University 2006;26(7):1053-1054
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo screen the peptide inhibitor of acetylcholinesterase (AChE) from 12-mer random phage display peptide library.
METHODSHuman AChE was used as the target to screen its binding peptides from 12-mer random phage display peptide library. The positive phage clones were isolated after three rounds of biopanning followed then by sequence analysis and their activity evaluation.
RESULTSSix positive phage clones binding to human AChE were obtained, and 4 of them sharing the conservative sequence W(S/P)HY inhibited the enzyme activity of AChE.
CONCLUSIONAcquisition of AChE inhibitor from phage display library provides clues for designing peptide inhibitors of AChE.