Drug Designing: Open Access
Open Access
ISSN: 2169-0138
ISSN: 2169-0138
Tareq Abu Izneid, Maria Vetro, Saud Bawazeer, Franck Fieschi, Anna Bernardi
Umm Al-Qura University, Saudi Arabia
Dept of Chemistry, Italy
Universite Grenoble-Alpes, France
Posters & Accepted Abstracts: Drug Des
DC-SIGN is a C-type lectin expressed on dendritic cells. It contains four Ca2+- dependent carbohydrate recognition domains that specifically recognize complex mannose glycans present on the surface of invading microorganisms. For some pathogens, including viruses like HIV, Ebola or Dengue [1], this recognition event contributes to infection transmission, making DC-SIGN a very interesting target for the design of antiviral agents. Dengue virus infection (DENV) is currently expanding worldwide since it is present in more than 128 countries in the world[2]. DENV is the most prevalent mosquitoborne viral disease causing clinical syndromes in humans. As there is no available vaccine or treatment, DENV infection has become a major international public health concern and the search for anti-dengue treatment is of extreme importance and it is an active field of research. Among the DC-SIGN antagonists reported in the literature, two mannose derivatives have drawn ourattention (Ligand I[3] and Ligand II[4]), which are two of the most potent monovalent mannose derived DCSIGN antagonists that are reported so far. The well-known weak binding affinity which characterizes carbohydrate-protein interactions, can be overcome by multivalent presentation. Based on the previous experience of our group, herein we discuss the synthesis of the two ligands I and II functionalized with an azido linker and their conjugation to a rod-core system[5] in order to prepare both hexa- and di-valent glycodendrimers as DC-SIGN antagonists.
Tareq Abu Izneid is working as professor at Umm Al Qura University in Saudi Arabia.
E-mail: tizneid@gmail.com