Document Type

Article

Publication Date

1-22-2024

Publication Title

International Journal of Molecular Science

Volume

25

Issue

2

Pages

1-22

Publisher Name

MDPI

Abstract

Based on our previous success in using cyclobutanone derivatives as enzyme inhibitors, we have designed and prepared a 37-member library of α-aminocyclobutanone amides and sulfonamides, screened for inhibition of the bacterial enzyme diaminopimelate desuccinylase (DapE), which is a promising antibiotic target, and identified several inhibitors with micromolar inhibitory potency. Molecular docking suggests binding of the deprotonated hydrate of the strained cyclobutanone, and thermal shift analysis with the most potent inhibitor (3y, IC50 = 23.1 µM) enabled determination of a Ki value of 10.2 +/− 0.26 µM and observed two separate Tm values for H. influenzae DapE (HiDapE).

Comments

Author Posting © The Authors, 2024. This is an open access article published by the International Journal of Molecular Science, Volume 25, Issue 2. https://doi.org/10.3390/ijms25021339

Creative Commons License

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

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Chemistry Commons

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