http://www.cnr.it/ontology/cnr/individuo/prodotto/ID39562
Probing specific protein recognition by size-controlled glycosylated cyclodextrin nanoassemblies (Articolo in rivista)
- Type
- Label
- Probing specific protein recognition by size-controlled glycosylated cyclodextrin nanoassemblies (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1039/b608495h (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- A. Mazzaglia; A. Valerio; V. Villari; A. Rencurosi; L. Lay; S. Spadaro; L. Monsù Scolaro; N. Micali (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto per lo Studio dei Materiali Nanostrutturati, ISMN-CNR,
Dipartimento di Chimica Inorganica, Chimica Analitica e Chimica
Fisica, Università di Messina, Salita Sperone 31, 98166 Messina,
Italy.
Dipartimento di Chimica Organica ed Industriale, Via G. Venezian
21, 20133 Milano, Italy
Istituto per i Processi Chimico Fisici, IPCF-CNR, Via La Farina,
237, 98123 Messina, Italy.
Istituto di Scienze e Tecnologie Molecolari, ISTM-CNR, Via C.
Golgi 19, 20133 Milano, Italy
Dipartimento di Fisica della Materia e Tecnologie Fisiche Avanzate,
Universita` di Messina, Contrada di Dio, S. Agata, 98166 Messina,
Italy
Dipartimento di Chimica Inorganica, Chimica Analitica e Chimica
Fisica, Universita` di Messina and C.I.R.C.M.S.B., Salita Sperone
31, 98166 Messina, Italy (literal)
- Titolo
- Probing specific protein recognition by size-controlled glycosylated cyclodextrin nanoassemblies (literal)
- Abstract
- The balance between hydrophobic and hydrophilic components in amphiphilic b-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. b-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 hydrophobichydrophilic balance of the
macrocycle labelled with targeting groups allows the design of active nanosized carriers for
drug delivery. (literal)
- Prodotto di
- Autore CNR
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