Beschreibung:
<jats:title>Abstract</jats:title><jats:p>CD1a protein binds sulfatide (3‐<jats:italic>O</jats:italic>‐sulfo‐β‐<jats:sc>D</jats:sc>‐galactosylceramide) to form an antigen complex that interacts with T cell receptors and activates T cells. To assess the role of the position of the sulfate in T cell activation, the synthesis of three β‐<jats:sc>D</jats:sc>‐galactosylceramides, variously bearing a sulfate at position 2, 4, or 6 of galactose, has been planned and carried out. The compounds were synthesized by an orthogonal sulfation strategy from a common β‐<jats:sc>D</jats:sc>‐galactosylceramide scaffold, which was in turn obtained through an efficient glycosylation reaction between a fully orthogonally protected galactosyl imidate and 3‐<jats:italic>O</jats:italic>‐benzoylazidosphingosine. Immunological evaluation of the three sulfated compounds in CD1a‐mediated T cell activation, in comparison with natural sulfatide, provided evidence of the influence of the sulfate position in the recognition event between the antigen, the CD1 protein and the T cell receptor.</jats:p>