The functionalization of liposomes with glycosylated amphiphiles is an optimal strategy for targeted drug delivery, leading to enhanced efficacy as well as to reduced side effects of drugs. In fact, the presence of natural or synthetic glycolipids in vesicle formulations might increase their specificity toward lectins, a class of non-enzymatic sugar-binding proteins involved in cellular recognition and adhesion. The capability of a new glucosylated synthetic amphiphile to interact with Concanavalin A (Con A), a plant lectin used as model system, was investigated by a synergic experimental and computational approach, both as pure component and in formulation with a natural phospholipid. The comparison of the affinity with Con A of the new glucosylated amphiphile with respect to that of a previously described structural analogue demonstrates that the hydrophilic spacer length controls the exposure of the glucose residue on liposome surface, and consequently the recognition by the lectin. © 2015 Elsevier B.V.
|Titolo:||Role of the hydrophilic spacer of glucosylated amphiphiles included in liposome formulations in the recognition of Concanavalin A|
|Data di pubblicazione:||2015|
|Appare nella tipologia:||01a Articolo in rivista|