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. 2024 Jun 30;25(13):7242. doi: 10.3390/ijms25137242

Figure 1.

Figure 1

Affinity study of αLa mAb 5B9 to La-derived synthetic peptides. The affinity of αLa mAb 5B9 to La-derived peptides was performed by PEPperMAP® epitope mapping. (A) Peptides with a peptide–peptide overlap of 14 aa were generated from the La protein. E5B9L sequence (“Peptide 3”) is indicated in bold and red. The 10 aa from the E5B9 peptide epitope are underlined. (B) Each aa of the wild-type peptide PSKPLPEVTDEYKND was replaced by the 20 standard aa, generating 300 peptides. The relative binding in percentage of the αLa mAb 5B9 to each of these peptides compared to the WT peptide is shown as a function of each substituted aa. Amino acids with different properties are color-coded as follows: polar (green), non-polar (black), aromatic (pink), negatively charged (red), and positively charged (blue).