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Enzymatic degradation of bovine serum albumin nanoparticles for drug delivery Open Access


Other title
bovine serum albumin
matrix metalloproteinase-2
Type of item
Degree grantor
University of Alberta
Author or creator
Singh, Harsh
Supervisor and department
Uludag, Hasan (Department of Chemical and Materials Engineering)
Unsworth, Larry D. (Department of Chemical and Materials Engineering)
Examining committee member and department
Unsworth, Larry D. (Department of Chemical and Materials Engineering)
Lange, Carlos F. (Department of Mechanical Engineering)
Uludag, Hasan (Department of Chemical and Materials Engineering)
Zeng, Hongbo (Department of Chemical and Materials Engineering)
Department of Chemical and Materials Engineering

Date accepted
Graduation date
Master of Science
Degree level
Coacervation is a mild process for developing protein NPs. Bovine serum albumin (BSA) NPs formed via this technique were stabilized using poly-L-Lysine (PLL); short interfering ribonucleic acid (siRNA) was used as a model drug for encapsulation. Specific and non-specific degradation of these coated and uncoated BSA NPs were carried using matrix metalloproteinase-2 (MMP-2) and trypsin, respectively. The particles were characterized with atomic force microscopy, zeta-potential, and photon correlation spectroscopy measurements. There was a significant increase in the zeta potential of BSA NPs upon coating. Trypsin digested the uncoated and coated BSA NPs and resulted in higher BSA release from the particles. However, MMP-2 treatment did not result in higher release of BSA from coated NPs despite the cleavability of coated polymer by MMP-2. This study described a method for obtaining BSA NPs in a controllable size range. Such particles showed degradability in the presence of trypsin and could be promising for targeted drug delivery applications.
License granted by Harsh Singh ( on 2009-12-22T05:40:16Z (GMT): Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of the above terms. The author reserves all other publication and other rights in association with the copyright in the thesis, and except as herein provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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