6533b871fe1ef96bd12d1976

RESEARCH PRODUCT

Not always what closes best opens better: mesoporous nanoparticles capped with organic gates

Ana M. CosteroPedro AmorósPablo GaviñaJamal El HaskouriRamón Martínez-máñezFélix SancenónMargarita ParraElena Añón

subject

Materials science102 Porous / Nanoporous / Nanostructured materialslcsh:BiotechnologyNanoparticle02 engineering and technologyGating010402 general chemistryEngineering and Structural Materials01 natural scienceslaw.inventionSilica nanoparticlesRhodamine 6Gchemistry.chemical_compoundlaw10 Engineering and Structural materialslcsh:TP248.13-248.65lcsh:TA401-492General Materials ScienceCalcinationgated nanodevices021001 nanoscience & nanotechnologyesterase controlled release0104 chemical sciencesChemical engineeringchemistrylcsh:Materials of engineering and construction. Mechanics of materials0210 nano-technologyMesoporous materialmesoporous nanoparticles

description

ABSTRACT Four types of calcined MCM-41 silica nanoparticles, loaded with dyes and capped with different gating ensembles are prepared and characterized. N1 and N2 nanoparticles are loaded with rhodamine 6G and capped with bulky poly(ethylene glycol) derivatives bearing ester groups (1 and 2). N3-N4 nanoparticles are loaded with sulforhodamine B and capped with self-immolative derivatives bearing ester moieties. In the absence of esterase enzyme negligible cargo release from N1, N3 and N4 nanoparticles is observed whereas a remarkable release for N2 is obtained most likely due to the formation of an irregular coating on the outer surface of the nanoparticles. In contrast, a marked delivery is found in N1, N3, and N4 in the presence of esterase enzyme. The delivery rate is related to the hydrophilic/hydrophobic character of the coating shell. The use of hydrophilic poly(ethylene glycol) derivatives as gating ensembles on N1 and N2 enables an easy access of esterase to the ester moieties with subsequent fast cargo release. On the other hand, the presence of a hydrophobic monolayer on N3 and N4 partially hinders esterase enzyme access to the ester groups and the rate of cargo release was decreased.

https://dx.doi.org/10.6084/m9.figshare.8325143.v1