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1H-n.m.r. studies of a natural immunoadjuvant peptidoglycan monomer: Proposed structure in solution in methyl sulfoxide

✍ Scribed by Branimir Klaić; Robert L. Domenick

Publisher
Elsevier Science
Year
1990
Tongue
English
Weight
508 KB
Volume
196
Category
Article
ISSN
0008-6215

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✦ Synopsis

The conformation in solution in methyl sulfoxide of the immunoadjuvant peptidoglycan monomer (PGM), obtained by digestion with lysozyme of the linear peptidoglycan polymer isolated from Brevibacaerium divaticatum, was studied by 'H-n.m.r. spectroscopy. The temperature dependence of the chemical shift of the resonances of the amide protons suggested that the amino group of alanine-is involved in hydrogen bonding, most probably to the cu-carbonyl of the isoglutamine which showed restricted rotation, as indicated by the large chemical shift nonequivalence for the resonances of the PCH, group. A cyclic structure is proposed for the C-terminal pentapeptide of PGM, which is further supported by various n.0.e. interactions involving the meso-diaminopimelic residue and the N-acetylmuramoyl group.

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