Structural Characterization of the Highly Cyclized
Lantibiotic Paenicidin A via a Partial Desulfurization/Reduction Strategy
Christopher
T. Lohans
Zedu Huang
Marco J. van Belkum
Maude Giroud
Clarissa S. Sit
Erika M. Steels
Jing Zheng
Randy
M. Whittal
Lynn M. McMullen
John C. Vederas
10.1021/ja3089229.s001
https://acs.figshare.com/articles/journal_contribution/Structural_Characterization_of_the_Highly_Cyclized_Lantibiotic_Paenicidin_A_via_a_Partial_Desulfurization_Reduction_Strategy/2463997
Lantibiotics
are ribosomally synthesized antimicrobial peptides
produced by bacteria that are increasingly of interest for food preservation
and possible therapeutic uses. These peptides are extensively post-translationally
modified, and are characterized by lanthionine and methyllanthionine
thioether cross-links. <i>Paenibacillus polymyxa</i> NRRL
B-30509 was found to produce polymyxins and tridecaptins, in addition
to a novel lantibiotic termed paenicidin A. A bacteriocin termed SRCAM
602 previously reported to be produced by this organism and claimed
to be responsible for inhibition of <i>Campylobacter jejuni</i> could not be detected either directly or by genomic analysis. The
connectivities of the thioether cross-links of paenicidin A were solved
using a novel partial desulfurization/reduction strategy in combination
with tandem mass spectrometry. This approach overcame the limitations
of NMR-based structural characterization that proved mostly unsuccessful
for this peptide. Paenicidin A is a highly cyclized lantibiotic, containing
six lanthionine and methyllanthionine rings, three of which are interlocking.
2012-12-05 00:00:00
food preservation
Cyclized Lantibiotic Paenicidin
Campylobacter jejuni
cyclized lantibiotic
antimicrobial peptides
NRRL
tandem mass spectrometry
Structural Characterization
novel lantibiotic
thioether
genomic analysis
SRCAM 602
methyllanthionine rings
paenicidin