Journal article
Somnogenic activity of O-acetylated and dimeric muramyl peptides
Infection and immunity, Vol.57(9), pp.2726-2732
09/1989
Handle:
https://hdl.handle.net/2376/104498
PMCID: PMC313518
PMID: 2759708
Abstract
Slow-wave sleep-promoting factors in brain and urine were identified as muramyl peptides (MPs), the building blocks of bacterial cell wall peptidoglycan. In this study, structural variations of MPs that occur naturally in bacterial peptidoglycan were investigated for somnogenic activity. Monomeric and dimeric MPs were isolated and purified from Neisseria gonorrhoeae and Actinomadura sp. strain R39. The structures of these MPs were verified by fast atom bombardment mass spectroscopy and tandem mass spectroscopy. After intracerebroventricular administration of MPs, electroencephalograms and brain temperatures of rabbits were recorded for 6 h and were analyzed to determine durations of slow-wave sleep, rapid-eye-movement sleep, and wakefulness. The 6-O acetylation of muramic acid enhanced the somnogenic effects of certain monomeric MPs relative to their non-O-acetylated (but otherwise identical) counterparts. Two monomeric MPs containing an unsubstituted amide (i.e., Iso-Gln) were inactive, thus confirming previous results showing that amidation of a variety of MPs can block somnogenic activity. Two peptide-cross-linked MP dimers tested had no effect on slow-wave sleep, although a third peptide-cross-linked MP containing a 1,6-anhydro muramyl end on one of its monomeric subunits, a structure that enhances somnogenic potency of un-cross-linked monomers, was somnogenic. Two dimers connected by glycosidic bonds and containing an Iso-Gln moiety were inactive. Two other glycosidically linked dimers that also contained an Iso-Gln moiety, but were of lower molecular weight, were somnogenic. In summary, 6-O acetylation of muramic acid in somnogenic MPs enhances activity, and as a class, peptide-linked dimeric MPs tend to be less active than their constituent monomers.
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Details
- Title
- Somnogenic activity of O-acetylated and dimeric muramyl peptides
- Creators
- L Johannsen - Department of Physiology and Biophysics, University of Tennessee, Memphis 38163R S Rosenthal - Department of Physiology and Biophysics, University of Tennessee, Memphis 38163S A Martin - Department of Physiology and Biophysics, University of Tennessee, Memphis 38163A B Cady - Department of Physiology and Biophysics, University of Tennessee, Memphis 38163F Obal - Department of Physiology and Biophysics, University of Tennessee, Memphis 38163M Guinand - Department of Physiology and Biophysics, University of Tennessee, Memphis 38163J M Krueger - Department of Physiology and Biophysics, University of Tennessee, Memphis 38163
- Publication Details
- Infection and immunity, Vol.57(9), pp.2726-2732
- Academic Unit
- Integrative Physiology and Neuroscience, Department of
- Identifiers
- 99900546778101842
- Language
- English
- Resource Type
- Journal article