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Table 1. Stimulation of antibody production to ovalbumine *SubstanceFold over controlGMDP 6.09±2.32GMDP 95% alfa-anomer 1.35±1.2GMDP 82% beta-anomer 5.87±2.62GMDP + Gly-Sar (1:10 mol/mol) 6.2±1.93GMDP + GlcNac (1:10 mol/mol) 0.84±0.19Gly-Sar 0.84±0.38GlcNac 1.01±0.26*BALB/c, 6 animals/group, each mouse was immunized by25µg OVA and 0.144µM ofGMDP sample i.p. Two boostings were done with 12.5µg OVA only. Antiserum from eachmouse was tested by ELISA. Control group received only OVA.Rate of GMDP anomers conversion.The investigation of rate GMDP anomers conversion by analytical HPLC revealedthat for isolated samples with 82% beta- and 95% alfa-anomers standard equilibrium state(30% beta- and 70% alfa-anomers) in solution arose not so fast as we thought earlier: 82%beta-anomer 40 min later of dissolution converted only to 59.6% beta-anomer and standardGMDP anomer’s equilibrium was achieved during 120 min interval. This rate of GMDPanomer’s conversion was enough for studying of presumed difference in biologicalactivities of alfa- and beta- anomers.Adjuvant activities of alfa- and beta-anomers of GMDP.We measured in vivo stimulation of antibody production by 82% beta- and 95%alfa-anomers GMDP samples in comparison with standard GMDP sample (30% beta- and70% alfa-anomers). Obtained results showed (Table 1) that adjuvant activities of 82% betaanomerand standard sample of GMDP were equal but 95% alfa-anomer did notdemonstrate adjuvant activity.Influence of GMDP competition with Gly-Sar and GlcNac on adjuvant activity.We suggested that such strong conformational restriction of GMDP activitydemonstrated above might be related to receptor binding specificity or existence of specialsterical gate of GMDP transport system. In order to highlight the mechanism of GMDPuptake we measured the adjuvant activity of standard GMDP sample in the presence ofGly-Sar (agonist of peptide transporter PEPT1) and N-acetylglucosamine (GlcNac,terminal part of saccharide unit of GMDP) which possibly interferes with carbohydratetransporter(s). We concluded from data Table 1 that Gly-Sar was inactive while GlcNaccompletely inhibited the GMDP activity.Taking together, the data obtained direct further research to investigation of possibleGMDP phosphorylation by GlcNac kinase since this enzyme demonstrates high preferencefor the beta-anomer of GlcNac [2].AcknowledgmentsThis work was supported by joint stock company “PEPTEK”.References1. Meshcheryakova, E., et al. Vaccine 25, 4515-4520 (2007).2. Blume, A., et al. Biochemistry 47, 13138-13146(2008).551