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Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody.
- Source :
-
Chemical communications (Cambridge, England) [Chem Commun (Camb)] 2020 Dec 08; Vol. 56 (96), pp. 15137-15140. - Publication Year :
- 2020
-
Abstract
- The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody's contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design of peptide-mimetics for developing efficient anti-cancer vaccines and diagnostic tools.
- Subjects :
- Antibodies, Monoclonal pharmacology
Antineoplastic Agents pharmacology
Cancer Vaccines pharmacology
Drug Screening Assays, Antitumor
Glycopeptides chemistry
Glycosylation
Humans
Hydrogen Bonding
Lectins pharmacology
Molecular Dynamics Simulation
Peptide Fragments chemistry
Protein Conformation
Structure-Activity Relationship
Antibodies, Monoclonal chemistry
Antineoplastic Agents chemistry
Cancer Vaccines chemistry
Lectins chemistry
Mucin-1 chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1364-548X
- Volume :
- 56
- Issue :
- 96
- Database :
- MEDLINE
- Journal :
- Chemical communications (Cambridge, England)
- Publication Type :
- Academic Journal
- Accession number :
- 33211039
- Full Text :
- https://doi.org/10.1039/d0cc06349e