Abstract
A series of new muramyl dipeptide (MDP) mimics were designed and synthesized via a solid-phase synthetic route. Their adjuvant activities were evaluated ex vivo for investigation of the synergism of the S(28-39) peptide, which is an MHC class I binding epitope of recombinant hepatitis B surface antigen (HBsAg) for both humans and mice. Several compounds without the carbohydrate moiety exerted better adjuvanticity than the MDP-C that has been reported by our laboratory previously. A primary screening test revealed that compounds 6, 14 and 16 exhibited stronger adjuvanticity compared with other MDP mimics.
Copyright © 2011 Elsevier Ltd. All rights reserved.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Acetylmuramyl-Alanyl-Isoglutamine / chemical synthesis
-
Acetylmuramyl-Alanyl-Isoglutamine / chemistry*
-
Acetylmuramyl-Alanyl-Isoglutamine / immunology
-
Adjuvants, Immunologic
-
Amino Acid Sequence
-
Animals
-
Carbohydrates / chemistry
-
Hepatitis B Surface Antigens / chemistry
-
Hepatitis B Surface Antigens / genetics
-
Hepatitis B Surface Antigens / metabolism
-
Hepatitis B Vaccines / immunology*
-
Mice
-
Mice, Inbred BALB C
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / genetics
-
Recombinant Proteins / metabolism
-
Structure-Activity Relationship
Substances
-
Adjuvants, Immunologic
-
Carbohydrates
-
Hepatitis B Surface Antigens
-
Hepatitis B Vaccines
-
Recombinant Proteins
-
Acetylmuramyl-Alanyl-Isoglutamine