Structures of biologically active muramyl peptides from peptidoglycan of Streptococcus sanguis

Sarka Beranova, Dominic M. Desiderio, Michael J. Pabst

Research output: Contribution to journalArticle

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Abstract

The structures of major muramyl peptides derived from peptidoglycan of the oral pathogen Streptococcus sanguis were determined and the biological activity of the peptides was tested in vitro on human monocytes. The muramyl peptides, produced by muramidase digestion of the purified peptidoglycan, were separated by reversed-phase high-performance liquid chromatography, either in their native form or after reduction with sodium borohydride. Chemical structures of the peptides were elucidated by a combination of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, amino acid analysis, post-source decay analysis and Edman sequencing. The study revealed two distinct monomers: N-acetylglucosaminyl-N-acetylmuramyl-Ala-iGln-Lys(Ala-Ala) (1), where the Ala-Ala is connected to the ε-group of lysine, and N-acetylglucosaminyl-N-acetylmuramyl-Ala-iGln-Lys(Ala-Ala)-Ala-Ala (2), where an additional dialanyl residue is attached to the lysine α-carboxyl group. Two sets of higher oligomers (di-, tri- and tetramers), related structurally to monomers 1 or 2 were also detected. In these oligomers, the monomeric subunits are linked together by Ala-Ala-Ala bridges. The native muramyl peptides primed human monocytes in vitro for the increased production of the microbicidal superoxide radical.

Original languageEnglish (US)
Pages (from-to)1182-1191
Number of pages10
JournalJournal of Mass Spectrometry
Volume33
Issue number12
DOIs
StatePublished - Dec 1 1998

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Peptidoglycan
Peptides
Oligomers
Lysine
Monomers
High performance liquid chromatography
Pathogens
Muramidase
Bioactivity
Superoxides
Ionization
Mass spectrometry
Desorption
Amino Acids
Lasers

All Science Journal Classification (ASJC) codes

  • Spectroscopy

Cite this

Structures of biologically active muramyl peptides from peptidoglycan of Streptococcus sanguis. / Beranova, Sarka; Desiderio, Dominic M.; Pabst, Michael J.

In: Journal of Mass Spectrometry, Vol. 33, No. 12, 01.12.1998, p. 1182-1191.

Research output: Contribution to journalArticle

Beranova, Sarka ; Desiderio, Dominic M. ; Pabst, Michael J. / Structures of biologically active muramyl peptides from peptidoglycan of Streptococcus sanguis. In: Journal of Mass Spectrometry. 1998 ; Vol. 33, No. 12. pp. 1182-1191.
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