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. Author manuscript; available in PMC: 2023 Aug 30.
Published in final edited form as: J Am Chem Soc. 2022 Nov 17;144(47):21628–21639. doi: 10.1021/jacs.2c09004

Figure 6: Ester and aspartimide formation in disulfide-substituted amycolimiditide variants.

Figure 6:

A: Esterification of disulfide-substituted AmdA variants in vitro by AmdB for 20 h at RT. The presence of a disulfide bond that constrains the peptide (-DTT spectra) inhibits esterification whereas reduced, unconstrained substrates are esterified efficiently. A reaction with wild-type AmdA (4 h at RT) is shown as a control. B: Time course of in vitro as partimidylation of pre-amycolimiditide variants with and without disulfide bonds by AmdM. All reactions were initiated with 10 μM peptide, but a mass spectrum was not acquired at the 0 min timepoint. The presence of disulfide bonds has minimal effect on the rate of methylation/aspartimidylation.