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mAb Peptide Map

Figure 1 below illustrates the 62 resulting Herceptin (trastuzumab) peptides following trypsin digestion; 20 from the light chains (Lc) and 42 from the heavy chains (Hc).

Herceptin peptides following trypsin digestion

Figure 1: Herceptin peptides following trypsin digestion.

The characteristic terminal Lys/K and Arg/R residues can be seen, and it is noteworthy that the resulting peptides range in size markedly from single amino acids – T9 and T37 – up to very long peptide chains – T35 and T7 which contain 63 and 37 amino acid residues respectively. It does not correlate perfectly, as it is dependent on the specific amino acids present, but typically the smaller the peptide the more polar and the more difficult to retain under reversed phase conditions.

Conversely, the longer the peptide, the more hydrophobic and the more retentive it will be under the same conditions. The fact that both highly polar/hydrophilic and hydrophobic peptides can be successfully chromatographed on the same analytical column, and under identical conditions, with high chromatographic efficiency showcases the power of RPLC.

 
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