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. 2024 May 20;25(3):bbae247. doi: 10.1093/bib/bbae247

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© The Author(s) 2024. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Binding evaluation of the pHLA complexes for HPV peptides. (A) Visualization of the pHLA complexes for the original (ELQRREVYK) and mutated (ALQRREVYK) peptides using PyMOL, with the statistics of the bonding interactions at the bottom. (B) Flow cytometry results show a leftward shift in the fluorescence intensity for the mutated peptide (ALQRREVYK), indicating its enhanced binding affinity to the HLA-A^*11:01 allele in contrast to the original peptide (ELQRREVYK), which does not exhibit a discernible shift. The negative control is the experiment without competitor peptides, and the positive control is the one with an unlabeled positive control peptide. (C) Summarized binding affinity and competitive inhibition percentages of peptides with the HLA-A^*11:01 allele.