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ACS Chem Biol. 2014 Feb 21;9(2):398-404. doi: 10.1021/cb400692w. Epub 2013 Nov 20.

A glycosylated, labionin-containing lanthipeptide with marked antinociceptive activity.

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1
NAICONS Srl , Via Fantoli 16/15, 20138 Milano, Italy.

Abstract

Among the growing family of ribosomally synthesized, post-translationally modified peptides, particularly intriguing are class III lanthipeptides containing the triamino acid labionin. In the course of a screening program aimed at finding bacterial cell wall inhibitors, we discovered a new lanthipeptide produced by an Actinoplanes sp. The molecule, designated NAI-112, consists of 22 amino acids and contains an N-terminal labionin and a C-terminal methyl-labionin. Unique among lanthipeptides, it carries a 6-deoxyhexose moiety N-linked to a tryptophan residue. Consistently, the corresponding gene cluster encodes, in addition to the LanKC enzyme characteristic of this lanthipeptide class, a glycosyl transferase. Despite possessing weak antibacterial activity, NAI-112 is effective in experimental models of nociceptive pain, reducing pain symptoms in mice in both the formalin and the chronic constriction injury tests. Thus, NAI-112 represents, after the labyrinthopeptins, the second example of a lanthipeptide effective against nociceptive pain.

PMID:
24191663
DOI:
10.1021/cb400692w
[Indexed for MEDLINE]
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