The balance between hydrophobic and hydrophilic components in amphiphilic beta-cyclodextrins, targeted by receptor specific groups (SC6CDGlc, SC6CDGal, SC16CDGlc, SC16CDGal), sensitively influences the structural properties of these systems. The different amphiphilic features of single cyclodextrins generate micellar aggregates and vesicles with an internal aqueous compartment able to encapsulate guests, such as rhodamine 6G. Small-angle light scattering (SAXS), cryo-TEM and AFM investigations describe the size and shape of these self-organized glycoligands. Recognition of the nanoassemblies by a specific receptor has effectively been demonstrated by means of time resolved fluorescence and is addressed in water by the morphological properties of cyclodextrin aggregates. Exclusively galactosylated thiohexylcyclodextrin binds specifically lectin from Pseudomonas aeruginosa. beta-D-Galactose competes with galactosylated cyclodextrin aggregates by inhibiting lectin binding but does not affect the mesoscopic environment of the protein. The better selectivity of the less hydrophobic cyclodextrins towards lectin should probably be ascribed to the morphology (size and shape) of these cyclodextrin aggregates. The recognition properties of this particular cyclodextrin (SC6CDGal) are probably due to the presence of small micelles which interact more efficiently with the lectin binding site. The modulation of the hydrophobic-hydrophilic balance of the macrocycle labelled with targeting groups allows the design of "active" nanosized carriers for drug delivery.
|Titolo:||Probing specific protein recognition by size-controlled glycosylated cyclodextrin nanoassemblies|
VALERIO, ANTONIO MARCO (Secondo)
|Settore Scientifico Disciplinare:||Settore CHIM/06 - Chimica Organica|
|Data di pubblicazione:||2006|
|Digital Object Identifier (DOI):||10.1039/b608495h|
|Appare nelle tipologie:||01 - Articolo su periodico|