@article{06afcdab05894cfd8f0fc9344a752958,
title = "Incorporation of Nonproteinogenic Amino Acids in Class i and II Lantibiotics",
abstract = "Lantibiotics are ribosomally synthesized and post-translationally modified peptide natural products that contain thioether cross-links formed by lanthionine and methyllanthionine residues. They exert potent antimicrobial activity against Gram-positive bacteria. We herein report production of analogues of two lantibiotics, lacticin 481 and nisin, that contain nonproteinogenic amino acids using two different strategies involving amber stop codon suppression technology. These methods complement recent alternative approaches to incorporate nonproteinogenic amino acids into lantibiotics.",
author = "Nidhi Kakkar and Perez, {Jessica G.} and Liu, {Wenshe R.} and Jewett, {Michael C.} and {Van Der Donk}, {Wilfred A.}",
note = "Funding Information: *E-mail: vddonk@illinois.edu. ORCID Wenshe R. Liu: 0000-0002-7078-6534 Wilfred A. van der Donk: 0000-0002-5467-7071 Author Contributions N.K. and W.A.V. designed the study. N.K. performed all experiments. J.G.P., W.R.L., and M.C.J. provided reagents and strains. Funding This work was supported by the National Institutes of Health (R37 GM 058822 to W.A.V.), the Human Frontiers Science Program (Grant RGP0015/2017 to M.C.J.), and the National Science Foundation (MCB-1716766 to M.C.J.). J.G.P. was funded by a National Science Foundation Graduate Research Fellowship. A Bruker UltrafleXtreme MALDI TOF/TOF mass spectrometer was purchased in part with a grant from the National Institutes of Health (S10 RR027109). Notes The authors declare no competing financial interest. Publisher Copyright: {\textcopyright} 2018 American Chemical Society.",
year = "2018",
month = apr,
day = "20",
doi = "10.1021/acschembio.7b01024",
language = "English (US)",
volume = "13",
pages = "951--957",
journal = "ACS Chemical Biology",
issn = "1554-8929",
publisher = "American Chemical Society",
number = "4",
}