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Epidermin is a type A lantibiotic that is a tetracyclic 21-amino-acid peptide which contains meso-lanthionine, 3-methyllanthionine, and S-(2-aminovinyl)-D-cysteine. It is obtained from Staphylococcus epidermidis Tue 3298 and exhibits antibiotic activity against many Gram-positive bacteria. It has a role as a metabolite and an antibacterial agent.

Functional Peptides
Catalog number
CAS number
Molecular Formula
Molecular Weight
Staphylococcin 1580
Soluble in Methanol, Water
InChI Key
Canonical SMILES
1. Complete sequences of epidermin and nukacin encoding plasmids from oral-derived Staphylococcus epidermidis and their antibacterial activity
Kenta Nakazono, Mi Nguyen-Tra Le, Miki Kawada-Matsuo, Noy Kimheang, Junzo Hisatsune, Yuichi Oogai, Masanobu Nakata, Norifumi Nakamura, Motoyuki Sugai, Hitoshi Komatsuzawa PLoS One. 2022 Jan 18;17(1):e0258283. doi: 10.1371/journal.pone.0258283. eCollection 2022.
Staphylococcus epidermidis is a commensal bacterium in humans. To persist in the bacterial flora of the host, some bacteria produce antibacterial factors such as the antimicrobial peptides known as bacteriocins. In this study, we tried to isolate bacteriocin-producing S. epidermidis strains. Among 150 S. epidermidis isolates from the oral cavities of 287 volunteers, we detected two bacteriocin-producing strains, KSE56 and KSE650. Complete genome sequences of the two strains confirmed that they carried the epidermin-harboring plasmid pEpi56 and the nukacin IVK45-like-harboring plasmid pNuk650. The amino acid sequence of epidermin from KSE56 was identical to the previously reported sequence, but the epidermin synthesis-related genes were partially different. The prepeptide amino acid sequences of nukacin KSE650 and nukacin IVK45 showed one mismatch, but both mature peptides were entirely similar. pNuk650 was larger and had an additional seven ORFs compared to pIVK45. We then investigated the antibacterial activity of the two strains against several skin and oral bacteria and found their different activity patterns. In conclusion, we report the complete sequences of 2 plasmids coding for bacteriocins from S. epidermidis, which were partially different from those previously reported. Furthermore, this is the first report to show the complete sequence of an epidermin-carrying plasmid, pEpi56.
2. Epidermin and gallidermin: Staphylococcal lantibiotics
Friedrich Götz, Silvana Perconti, Peter Popella, Rolf Werner, Martin Schlag Int J Med Microbiol. 2014 Jan;304(1):63-71. doi: 10.1016/j.ijmm.2013.08.012. Epub 2013 Sep 4.
The Staphylococcus epidermidis derived epidermin was the first lantibiotic that has been shown to be ribosomally synthesized and posttranslationally modified. Together with gallidermin, produced by Staphylococcus gallinarum, they belong to the large class of cationic antimicrobial peptides (CAMPs) that act against a broad spectrum of Gram-positive bacteria. Here we describe the genetic organization, biosynthesis and modification, excretion, extracellular activation of the modified pre-peptide by proteolytic processing, self-protection of the producer, gene regulation, structure, and the mode of action of gallidermin and epidermin. We also address mechanisms of bacterial tolerance to these lantibiotics and other CAMPs. Particularly gallidermin has a high potential for therapeutic application, as it is active against methicillin-resistant Staphylococcus aureus strains (MRSA) and as it is able to prevent biofilm formation at sublethal concentrations.
3. Molecular Dynamics Insight into the Lipid II Recognition by Type A Lantibiotics: Nisin, Epidermin, and Gallidermin
Irina Panina, Amir Taldaev, Roman Efremov, Anton Chugunov Micromachines (Basel). 2021 Sep 28;12(10):1169. doi: 10.3390/mi12101169.
Lanthionine-containing peptides (lantibiotics) have been considered as pharmaceutical candidates for decades, although their clinical application has been restricted. Most lantibiotics kill bacteria via targeting and segregating of the cell wall precursor-membrane-inserted lipid II molecule-in some cases accompanied by pores formation. Nisin-like lantibiotics specifically bind to pyrophosphate (PPi) moiety of lipid II with their structurally similar N-terminal thioether rings A and B. Although possessing higher pore-forming capability, nisin, in some cases, is 10-fold less efficient in vivo as compared to related epidermin and gallidermin peptides, differing just in a few amino acid residues within their target-binding regions. Here, using molecular dynamics simulations, we investigated atomistic details of intermolecular interactions between the truncated analogues of these peptides (residues 1-12) and lipid II mimic (dimethyl pyrophosphate, DMPPi). The peptides adopt similar conformation upon DMPPi binding with backbone amide protons orienting into a single center capturing PPi moiety via simultaneous formation of up to seven hydrogen bonds. Epidermin and gallidermin adopt the complex-forming conformation twice as frequent as nisin does, enhancing the binding by the lysine 4 side chain. Introduction of the similar residue to nisin in silico improves the binding, providing ideas for further design of prototypic antibiotics.

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