In this article, we describe the design, synthesis and activity evaluation of glycomimetic DC-SIGN antagonists, that use a mannose residue to anchor to the protein carbohydrate recognition domain (CRD). The molecules were designed from the structure of the known pseudo-mannobioside antagonist 1, by including additional hydrophobic groups, which were expected to engage lipophilic areas of DC-SIGN CRD. The results demonstrate that the synthesized compounds potently inhibit DC-SIGN-mediated adhesion to mannan coated plates. Additionally, in silico docking studies were performed to rationalize the results and to suggest further optimization.
Design, synthesis and activity evaluation of mannose-based DC-SIGN antagonists / N. Obermajer, S. Sattin, C. Colombo, M. Bruno, U. Švajger, M. Anderluh, A. Bernardi. - In: MOLECULAR DIVERSITY. - ISSN 1381-1991. - 15:2(2011), pp. 347-360.
|Titolo:||Design, synthesis and activity evaluation of mannose-based DC-SIGN antagonists|
|Parole Chiave:||Anti-infectives; Carbohydrates; DC-SIGN; Dendritic cell-based assay; Glycoconjugates; Glycomimetics|
|Settore Scientifico Disciplinare:||Settore CHIM/06 - Chimica Organica|
|Data di pubblicazione:||2011|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1007/s11030-010-9285-y|
|Appare nelle tipologie:||01 - Articolo su periodico|