Peptide mimics of hapten DNP: The effect of affinity of anti-DNP monoclonal antibodies for the selection of phage-displayed mimotopes


Kalaycioglu A. T., Russell P. H., Howard C. R.

JOURNAL OF IMMUNOLOGICAL METHODS, vol.366, no.1-2, pp.36-42, 2011 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 366 Issue: 1-2
  • Publication Date: 2011
  • Doi Number: 10.1016/j.jim.2011.01.004
  • Journal Name: JOURNAL OF IMMUNOLOGICAL METHODS
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.36-42
  • Keywords: Phage-displayed libraries, 2-4 Dinitrophenol, Hapten, Mimotopes, SPOT SYNTHESIS, LIBRARIES, VIRUS, IDENTIFICATION, PURIFICATION, FRAGMENT, VACCINES, RECEPTOR, BINDING, ARRAYS
  • Karadeniz Technical University Affiliated: No

Abstract

Biopanning of two linear (6- and 15-mer) and two constrained (10- and 17-met) phage-displayed peptide libraries with two anti-DNP monoclonal antibodies (mAbs) selected seven unique peptide sequences using only the low affinity anti-DNP monoclonal antibody. The selected peptides contained two of 6, one of 10, two of 15 and two of 17 amino acids in length. They were all rich in hydrophobic residues. Both 15-mer peptides had antigenic regions of eight amino acids as revealed by a spot scan assay. Two of the 17-mer and one of the 10-mer peptides displayed on phage competed with free DNP for the low affinity anti-DNP mAb. These findings highlight (i) the selective power of phage displayed peptide libraries to identify peptides that mimic the shape of a small hapten molecule such as DNP, (ii) the possible preferential bias of phage libraries towards low affinity antibodies, (iii) the importance of using a panel of phage libraries for selecting peptide mimics. (C) 2011 Elsevier B.V. All rights reserved.