Characterization of a phage library displaying random 22mer peptides

Seung Joo Lee, Jeong Hwan Lee, Brian K. Kay, Gideon Dreyfuss, Yong Keun Park, Jeong Kook Kim

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


We have characterized a phage library displaying random 22mer peptides which were produced as N-terminal fusions to the pIII coat protein of M13 filamentous phages. Among the sixty phages randomly picked from the library, 25 phages had the 22mer peptide inserts. The DNA sequence analysis of the 25 inserts showed the following results: first, each nucleotide was represented almost equally at each codon position except that there were some biases toward G bases at the first position of the codons. Secondly, the expected 47 sense codons were represented. The deduced amino acid sequences of the 25 inserts were analyzed to examine its diversity. Glycine and glutamate were the two most overrepresented residues above the expected value, whereas cysteine and threonine residues were underrepresented. The range of diversity in dipeptide sequences showed that the amino acid residues were randomly distributed along the peptide insert. Acidic, basic, polar, and nonpolar amino acid residues were represented to the extent expected at most positions of the peptide inserts. The predicted isoelectric points and hydropathy indices of the 25 peptides showed that a variety of the peptides were represented in the library. These results indicate that this phage display library could be useful in fiuding ligands for a broad spectrum of receptors by affinity screening.

Original languageEnglish
Pages (from-to)347-353
Number of pages7
JournalJournal of Microbiology
Issue number4
Publication statusPublished - 1997 Dec


  • E. Coli
  • M13 bacteriophage
  • Peptide
  • Phage display library
  • pIII coat protein

ASJC Scopus subject areas

  • Microbiology
  • Applied Microbiology and Biotechnology


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