Selection of Trypsin Inhibitors in Phage Peptide Library

The newly developed techniques of peptide libraries have become a conventional and efficient method in screening ligands of proteins of interest. We present here the successful results of selection of trypsin inhibitors in a phage hexapeptide library. After affinity selection and activity assay, pep...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1996-03, Vol.220 (1), p.53-56
Main Authors: Fang, Rui, Qi, Jie, Lu, Zhi-bin, Zhou, Hui, Li, Wei, Shen, Jiacong
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Escherichia coli - genetics
In Vitro Techniques
Inovirus - genetics
Molecular Sequence Data
Molecular Structure
Oligopeptides - chemistry
Oligopeptides - genetics
Oligopeptides - pharmacology
Protein Engineering
Trypsin Inhibitors - chemistry
Trypsin Inhibitors - genetics
Trypsin Inhibitors - pharmacology
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Summary:The newly developed techniques of peptide libraries have become a conventional and efficient method in screening ligands of proteins of interest. We present here the successful results of selection of trypsin inhibitors in a phage hexapeptide library. After affinity selection and activity assay, peptide sequences, deduced from DNA sequencing of the phage peptides with the most striking trypsin activity, share some common features with trypsin inhibitors reported. All of the phage peptides selected out and those native and synthetic trypsin inhibitors reported are composed of three parts: (a) positively charged part (Arg, Lys or their analogs); (b) polar part that may form hydrogen bonds with Ser in the active site of trypsin; (c) hydrophobic part that interacts with the nonpolar region of trypsin active site.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.0355