Detection of tumor-associated glycopeptides by Lectins: The peptide context modulates carbohydrate recognition

  1. Madariaga, D. 1
  2. Martinez-Sáez, N. 1
  3. Somovilla, V.J. 1
  4. Coelho, H. 1
  5. Valero-González, J. 1
  6. Castro-Lopez, J. 1
  7. Asensio, J.L. 1
  8. Jiménez-Barbero, J. 1
  9. Busto, J.H. 1
  10. Avenoza, A. 1
  11. Marcelo, F. 1
  12. Hurtado-Guerrero, R. 1
  13. Corzana, F. 1
  14. Peregrina, J.M. 1
  1. 1 Universidad de La Rioja
    info

    Universidad de La Rioja

    Logroño, España

    ROR https://ror.org/0553yr311

Aldizkaria:
ACS chemical biology

ISSN: 1554-8929

Argitalpen urtea: 2015

Alea: 10

Zenbakia: 3

Orrialdeak: 747-756

Mota: Artikulua

DOI: 10.1021/CB500855X SCOPUS: 2-s2.0-84925352558 WoS: WOS:000351558700013 GOOGLE SCHOLAR

Beste argitalpen batzuk: ACS chemical biology

Garapen Iraunkorreko Helburuak

Laburpena

Tn antigen (α-O-GalNAc-Ser/Thr) is a convenient cancer biomarker that is recognized by antibodies and lectins. This work yields remarkable results for two plant lectins in terms of epitope recognition and reveals that these receptors show higher affinity for Tn antigen when it is incorporated in the Pro-Asp-Thr-Arg (PDTR) peptide region of mucin MUC1. In contrast, a significant affinity loss is observed when Tn antigen is located in the Ala-His-Gly-Val-Thr-Ser-Ala (AHGVTSA) or Ala-Pro-Gly-Ser-Thr-Ala-Pro (APGSTAP) fragments. Our data indicate that the charged residues, Arg and Asp, present in the PDTR sequence establish noteworthy fundamental interactions with the lectin surface as well as fix the conformation of the peptide backbone, favoring the presentation of the sugar moiety toward the lectin. These results may help to better understand glycopeptide-lectin interactions and may contribute to engineer new binding sites, allowing novel glycosensors for Tn antigen detection to be designed. © 2014 American Chemical Society.