الفهرس 
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Abstract
Nanomedicine holds great interest over the past 20 years and
nanotechnology has improved both diagnostics and therapeutics in
several medical fields, including, but not limited to, oncology, cardiology,
and diabetology. Indeed, multiple conventional antidiabetic agents are
clinically approved for the treatment of Type 2 diabetes mellitus (T2DM)
for improving the lives of patients and slowing the progression of disease.
Alpha-glucosidase inhibitors (AGIs) have shown potential as effective
therapies in the clinic among other treatment strategies. In this work, one
such AGI, miglitol, was loaded into periodic mesoporous organosilica
nanoparticles (PMO NPs) to improve the compound’s antidiabetic
activity and minimize cytotoxicity. PMO NPs were initially constructed
through a sol–gel technique, and were used to encapsulate high payloads
of miglitol. TEM and DLS analysis revealed that both unloaded and
loaded PMO NPs were spherical in shape with a diameter range of 324-
370 nm and a relatively high surface negative charge ranging between –
22 to –35 mV. TGA, FTIR, PXRD analyses also confirmed the effective
loading of the drug into the PMO NPs (i.e., up to ca. 89.3% loading
efficiency). Release kinetics experiment showed minimum release of
drug from PMO, ensure major amount of drug remains associated with
PMO. A 30 mg/kg dose of both pure miglitol drug and miglitol-loaded
PMO (Mig-PMO) NPs were orally administered to diabetic rats and their
treatment progression was monitored as compared with both healthy rats
(positive control) and untreated diabetic rats (negative control). These
animal studies revealed that the PMO nanoparticles are nontoxic
consistent with in vitro results performed on RAW macrophages. Further,
the Mig-PMO NPs exhibited a prolonged antidiabetic effect by
lowering/controlling the blood glucose levels of diabetic rats over a 10 h
period as compared to a 2 h sustained effect from free miglitol. The
antidiabetic effect was positively correlated with inhibition of intestinal
alpha-glucosidase enzyme.