Title: Phage displayed 6-mer mimotopes with a consensus proline absent in the minimized linear wild-type epitope
Authors: Deroo, S ×
Fournier, P
Theisen, D
Brons, NHC
Deckmyn, Hans
Muller, CP #
Issue Date: May-1998
Publisher: Kluwer academic publ
Series Title: Letters in peptide science vol:5 issue:2-3 pages:159-162
Abstract: Phage displayed random 6-mer libraries were screened with a monoclonal antibody specific for a minimized 'linear' 7-mer epitope of the measles virus hemagglutinin protein. No clone with the wild-type sequence was selected and most clones contained a sequence motif not found in the wild-type sequence. Two mimotopes (LYMPQLS, SEMPQLP) were synthesized which inhibited binding to the measles virus 95-135 times better than a wild-type peptide. Sequence comparison of proteins with known 3D-structure indicates that the epitope corresponds to an alpha-helix, while the best mimotopes have no predicted helix propensity. The proline is thought to be required for inducing a turn necessary for mimicking part of the alpha-helix. The higher intrinsic stability of such a mimotope may explain its improved binding and may be more suitable in immunogenicity experiments.
ISSN: 0929-5666
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Chemistry, Campus Kulak Kortrijk
Interdisciplinary Research Facility Life Sciences, Campus Kulak Kortrijk
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science