Thermodynamic Switch in Binding of Adhesion/Growth Regulatory Human Galectin-3 to Tumor-Associated TF Antigen (CD176) and MUC1 Glycopeptides

@inproceedings{Rodrguez2015ThermodynamicSI,
  title={Thermodynamic Switch in Binding of Adhesion/Growth Regulatory Human Galectin-3 to Tumor-Associated TF Antigen (CD176) and MUC1 Glycopeptides},
  author={M Carmen R{\'i}os Rodr{\'i}guez and Svetlana Yegorova and Jean-Philippe Pitteloud and Anais E. Chavaroche and Sabine Andr{\'e} and Ana Ard{\'a} and Dimitriy Minond and Jes{\'u}s Jim{\'e}nez-Barbero and Hans-Joachim Gabius and Mar{\'e} Cudic},
  booktitle={Biochemistry},
  year={2015}
}
A shift to short-chain glycans is an observed change in mucin-type O-glycosylation in premalignant and malignant epithelia. Given the evidence that human galectin-3 can interact with mucins and also weakly with free tumor-associated Thomsen-Friedenreich (TF) antigen (CD176), the study of its interaction with MUC1 (glyco)peptides is of biomedical relevance. Glycosylated MUC1 fragments that carry the TF antigen attached through either Thr or Ser side chains were synthesized using standard Fmoc… CONTINUE READING