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Rational design of class I MHC ligands

Authors :
Didier Rognan
Angelika Daser
Leonardo Scapozza
Gerd Folkers
Source :
AIP Conference Proceedings.
Publication Year :
1995
Publisher :
AIP, 1995.

Abstract

From the knowledge of the three‐dimensional structure of a class I MHC protein, several non natural peptides were designed in order to either optimize the interactions of one secondary anchor amino acid with its HLA binding pocket or to substitute the non interacting part with spacer residues. All peptides were synthesized and tested for binding to the class I MHC protein in an in vitro reconstitution assay. As predicted, the non natural peptides present an enhanced binding to the HLA‐B27 molecule with respect to their natural parent peptides. This study constitutes the first step towards the rational design of non peptidic MHC ligands that should be very promising tools for the selective immunotherapy of autoimmune diseases.

Details

ISSN :
0094243X
Database :
OpenAIRE
Journal :
AIP Conference Proceedings
Accession number :
edsair.doi...........6cd740bc009c86aae8e8384ab64af07d
Full Text :
https://doi.org/10.1063/1.47772