Identification of peptides binding to Pisum sativum agglutinin from a phage-displayed random peptide library.
- Author:
Xiang ZHOU
1
;
Jin-biao ZHAN
;
Xian-rong MAO
;
Ke-yi WANG
Author Information
- Publication Type:Journal Article
- MeSH: Binding Sites; Peptide Library; Peptides; metabolism; Plant Lectins; metabolism; Protein Binding; Recombinant Proteins; metabolism
- From: Journal of Zhejiang University. Medical sciences 2005;34(5):412-416
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo obtain peptides binding specifically to Pisum sativum agglutinin (PSA) from a phage-displayed random peptide library.
METHODS(1) A phage-displayed random hexapeptide library was screened with PSA as target. (2) Dot blot was used to analyze the influence of the alpha-Met-D-mannoside on binding between PSA and phage-displayed peptides. (3) Three peptides (RMWSF, RYDYSY, LRLRQL) were selectively synthesized, and different concentrations were used to inhibit PSA and ConA binding to the HRP.
RESULTSThe enrichment occurred obviously after three rounds of screening. The insert sequences of amino acids, displayed on 22 phage DNAs from the third round of screening, were divided into three groups. The binding of phage-displayed peptides to PSA was specific as shown by dot blot and could be inhibited by alpha-Met-D-mannoside. LRLRQL was not dissolved in water. ARMWSF and RYDYSY inhibited binding of PSA to HRP, but failed to inhibit binding ConA to HRP.
CONCLUSIONThe binding site of peptides ARMWSF and RYDYSY is different to that of alpha-Met-D-mannoside.
