Table 1.
Human Peptide | Sequence | Gene | Modification |
---|---|---|---|
P:1 | STAPPVHNV | MUC1 | Degenerate TR |
P:16 | STAPTVHNV | MUC1 | Modified |
P: 2 | STAPT(Tn)VHNV | MUC1 | Glycosylated |
P:15 | SLAPPVHNV | MUC1 | Anchor-optimized |
P: 3 | SLAPTVHNV | MUC1 | Anchor-optimized |
P: 4 | SLAPT(Tn)VHNV | MUC1 | Glycosylated |
P: 9 | ALGSTAPPV | MUC1 | Degenerate TR |
P:10 | ALGST(Tn)APPV | MUC1 | Glycosylated |
P: 7 | SLSYTNPAV | MUC1 | Cytoplasmic tail |
P: 5 | LLLLTVLTV | MUC1 | Signal peptide |
P:11 | YRPGENLNL | None (Negative control) | |
P:12 | YLSGADLNL | CEA | None (Positive control) |
P:13 | GLCTLVAML | EBV | None (Positive control) |
P:14 | NLVPMVATV | CMV | None (Positive control) |
All peptides have been synthesized using Fmoc chemistry on a MilliGen 9050 Synthesizer (PerSeptive Biosystems). Tn modifications were introduced at the fifth amino acid position of the peptide by using Fmoc-Thr(GalNAc(Ac3)-α-D)-OH, which was purchased from Bachem Bioscience. Peptides were purified on the Beckman System Gold HPLC using a Jupiter Proteo C12 column (Phenomenex) and an acetonitrile gradient. Peptides were greater than 95% pure as determined by mass spectrometry. Modifications are noted in bold.