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Immobilization of therapeutic agents on magnetic iron oxide nanoparticles decreases binding to blood serum proteins and increases resistance to enzymatic cleavage


Julia Nowak Jary

A drug’s affinity for binding blood serum proteins, such as
albumin, determines a primary interaction affecting its
biological activity. Only the free unbound fraction of a drug
can induce a therapeutic effect. A range of effective
antimicrobial agents, such as peptides containing N3-(4-
methoxyfumaroyl)-L-2,3-diaminopropanoic acid (FMDP), are
known to be powerful inhibitors of fungal and bacterial growth
in vitro; nevertheless, the use of these compounds in clinics
has proven intractable due to their irreversible binding of
blood serum proteins, causing complete loss of their biological
activity. Nanoparticles are now widely tested as drug carriers.
The main purpose of the work was to investigate the
differences in physicochemical properties (solubility,
penetration capacity, lipophilicity) between acid-soluble drugs
in magnetic iron oxide nanoparticles and similar drugs in their
unprotected form. The synthesis of Fe3O4 magnetic iron
oxide nanoparticles containing (3-aminopropyl) triethoxysilane
(APTES) is made with selected adhesive drugs. The detected
nanostructures were detected using IR spectroscopy, atomic
force microscopy (AFM), vibrating sample magnetometry
(VSM) and dynamic light distribution techniques (DLS), as
well as the physicochemical properties of untreated drugs
were studied. Drug deficiency was measured using a flasksaturation
filling method. The discovery was measured using
dialysis membrane, a MWCO 50 kD with pores <10 nm.
Lipophilicity was measured separately by octanol. Drugs
showed better solubility and low pH values (pH 2.0 and 5.0)
and lower solubility and higher pH values (pH 6.5 and 7.5)
compared to compatible non-compliant drugs.

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