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. Author manuscript; available in PMC: 2020 Nov 1.
Published in final edited form as: J Mol Cell Cardiol. 2019 Sep 7;136:42–52. doi: 10.1016/j.yjmcc.2019.09.002

Figure 8: Synthetic and biologically made HcTnI-C27 peptides have similar epitope conformation in physiologic buffer.

Figure 8:

Normalized to the maximum binding of a pre-determined concentration of mAb TnI-1 to intact cardiac TnI immobilized on microtiter plate, the competition curves of serial dilutions of chemically synthesized and biologically made HcTnI-C27 peptides were nearly identical, reflecting their comparable epitope conformation in a physiologic buffer (A). Synthetic and biologically made HcTnI-C27-H mutant peptides both showed drastically diminished ability in competing for mAb TnI-1, reflecting similarly altered conformation of the epitope (B).