Muramyl peptides bind specifically to rat brain membranes.
The capability of immunoactive muramyl peptides to bind specifically to rat brain membranes has been discovered. The reaction of an N-acetylglucosaminylmuramyl dipeptide analog having an additional C-terminal lysine residue (GMDP-Lys) with Bolton-Hunter reagent or N-hydroxysuccinimidyl-4-azidosalicylate afforded two acylated derivatives, GMDP-Lys-(Hp) and GMDP-Lys(Azs). Their iodination resulted in radioactive derivatives (spec. act. approximately 2000 Ci/mmol) whose binding to rat brain membranes is characterized by Kd approximately 3 nM and Bmax approximately 10 fmol/mg membrane protein. Binding could be inhibited by muramyl dipeptide (MDP), GMDP-Lys, and GMDP, while fragments of the latter, N-acetylglucosamine dipeptide and disaccharide, were ineffective.
Kaydalov
A A
AA
Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow.
Utkin YuN
Andronova
T M
TM
Tsetlin
V I
VI
Ivanov
V T
VT
D000107:Acetylation; D000119:Acetylmuramyl-Alanyl-Isoglutamine / Q000031:analogs & derivatives / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D001921:Brain / Q000378:metabolism*; D008566:Membranes / Q000378:metabolism; D010446:Peptide Fragments / Q000494:pharmacology; D051381:Rats
D010446:Peptide Fragments; D000119:Acetylmuramyl-Alanyl-Isoglutamine