The binding of monosaccharides and short peptides to lymphocyte receptors (human CD69 and rat NKR-P1A) was first reported in 1994 and then in a number of subsequent publications. Based on this observation, numerous potentially high-affinity saccharide ligands have been synthesized over the last two decades in order to utilize their potential in antitumor therapy. Due to significant inconsistencies in their reported binding properties, we decided to re-examine the interaction between multiple ligands and CD69 or NKR-P1A. Using NMR titration and isothermal titration calorimetry we were unable to detect the binding of the tested ligands such as N-acetyl-D-hexosamines and oligopeptides to both receptors, which contradicts the previous observations published in more than twenty papers over the last fifteen years.

• MeSH
• Antigens, CD metabolism   MeSH
• Antigens, Differentiation, T-Lymphocyte metabolism   MeSH
• Rats MeSH
• Lectins, C-Type metabolism   MeSH
• Humans MeSH
• Oligopeptides chemical synthesis   pharmacology   MeSH
• Polysaccharides chemical synthesis   pharmacology   MeSH
• Receptors, Immunologic metabolism   MeSH
• Recombinant Proteins metabolism   MeSH
• Protein Binding MeSH
• Animals MeSH
• Check Tag
• Rats MeSH
• Humans MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Antigens, CD MeSH
• CD69 antigen MeSH Browser
• Antigens, Differentiation, T-Lymphocyte MeSH
• Klrb1a protein, rat MeSH Browser
• Lectins, C-Type MeSH
• Oligopeptides MeSH
• Polysaccharides MeSH
• Receptors, Immunologic MeSH
• Recombinant Proteins MeSH