1. Rational design of class I MHC ligands
- Author
-
Didier Rognan, Angelika Daser, Leonardo Scapozza, and Gerd Folkers
- Subjects
chemistry.chemical_classification ,biology ,Chemistry ,medicine.medical_treatment ,Rational design ,Binding pocket ,Immunotherapy ,Human leukocyte antigen ,Major histocompatibility complex ,In vitro ,Amino acid ,Class I MHC protein ,Biochemistry ,medicine ,biology.protein - 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.
- Published
- 1995
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