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Design, synthesis and activity evaluation of mannose-based DC-SIGN antagonists.

ABSTRACT: 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.

SUBMITTER: Obermajer N

PROVIDER: S-EPMC7089406 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature

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Design, synthesis and activity evaluation of mannose-based DC-SIGN antagonists.

Obermajer Nataša N Sattin Sara S Colombo Cinzia C Bruno Michela M Svajger Urban U Anderluh Marko M Bernardi Anna A

Molecular diversity 20101114 2

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 adhesio ...[more]

PMID: 21076980

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