PMID: 8595249Oct 1, 1995Paper

Structurally defined synthetic cancer vaccines: analysis of structure, glycosylation and recognition of cancer associated mucin, MUC-1 derived peptides

Glycoconjugate Journal
X LiuB M Longenecker

Abstract

Translation of an immune response into therapy is probably the toughest task in designing vaccines for cancer due to the heterogeneity of the cell surface antigens which display tremendous variations in glycoforms. Consequently, a small segment (antigen) of cancer-associated mucin, in spite of generating antigen-specific immune responses, may be limited in therapeutic value. It is important that the synthetic segment resembles the native cancer-associated mucin in both structure and conformation. Synthetic cancer associated mucin derived 16 amino acid peptide GVTSAPDTRPAPGSTA and its partially glycosylated forms have demonstrated specific binding to two monoclonal antibodies, B27.29 and BCP8, raised against the native cancer associated mucin, MUC-1 and a MUC-1 derived synthetic peptide, respectively. In spite of the structural similarities at the core peptide level of both glycosylated and unglycosylated peptides, it appears that partial glycosylation does not inhibit and even slightly enhances binding to the MAb B27.29 indicating that the glycosylated synthetic peptide more closely resembles the native mucin epitope recognized by MAb B27.29. From molecular dynamic simulations using NMR derived distance constraints, both glycos...Continue Reading

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Citations

May 7, 1999·International Journal of Immunopharmacology·J W Hadden
Aug 1, 1997·Current Opinion in Biotechnology·T Ben-Yedidia, R Arnon
Oct 26, 1999·The Journal of Peptide Research : Official Journal of the American Peptide Society·G A NaganagowdaM J Levine
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Nov 16, 2019·Journal of Peptide Science : an Official Publication of the European Peptide Society·Jaideep SinghCory L Brooks
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Feb 19, 2021·Drug Discovery Today·Vignesh Kamath
Jan 7, 2005·Biopolymers·Jason T SchumanA Patricia Campbell

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