1 research outputs found
Multilayer Capsules of Bovine Serum Albumin and Tannic Acid for Controlled Release by Enzymatic Degradation
With
the purpose to replace expensive and significantly cytotoxic positively
charged polypeptides in biodegradable capsules formed via Layer-by-Layer
(LbL) assembly, multilayers of bovine serum albumin (BSA) and tannic
acid (TA) are obtained and employed for encapsulation and release
of model drugs with different solubility in water: hydrophilic-tetramethylrhodamine-isothiocyanate-labeled
BSA (TRITC-BSA) and hydrophobic 3,4,9,10-tetra-(hectoxy-carbonyl)-perylene
(THCP). Hydrogen bonding is proposed to be predominant within thus
formed BSA/TA films. The TRITC-BSA-loaded capsules comprising 6 bilayers
of the protein and polyphenol are benchmarked against the shells composed
of dextran sulfate (DS) and poly-l-arginine (PARG) on degradability
by two proteolytic enzymes with different cleavage site specificity
(i.e., α-chymotrypsin and trypsin) and toxicity for murine RAW264.7
macrophage cells. Capsules of both types possess low cytotoxicity
taken at concentrations equal or below 50 capsules per cell, and evident
susceptibility to α-chymotrypsin resulted in release of TRITC-BSA.
While the BSA/TA-based capsules clearly display resistance to treatment
with trypsin, the assemblies of DS/PARG extensively degrade. Successful
encapsulation of THCP in the TRITC-BSA/TA/BSA multilayer is confirmed,
and the release of the model drug is observed in response to treatment
with α-chymotrypsin. The thickness, surface morphology, and
enzyme-catalyzed degradation process of the BSA/TA-based films are
investigated on a planar multilayer comprising 40 bilayers of the
protein and polyphenol deposited on a silicon wafer. The developed
BSA/TA-based capsules with a protease-specific degradation mechanism
are proposed to find applications in personal care, pharmacology,
and the development of drug delivery systems including those intravenous
injectable and having site-specific release capability