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Enzymatic degradation of bovine seru...
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Singh, Harsh Deep.
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Enzymatic degradation of bovine serum Albumin nanoparticles for drug delivery.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Enzymatic degradation of bovine serum Albumin nanoparticles for drug delivery./
作者:
Singh, Harsh Deep.
面頁冊數:
101 p.
附註:
Source: Masters Abstracts International, Volume: 48-03, page: 1728.
Contained By:
Masters Abstracts International48-03.
標題:
Chemistry, Pharmaceutical. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR55959
ISBN:
9780494559598
Enzymatic degradation of bovine serum Albumin nanoparticles for drug delivery.
Singh, Harsh Deep.
Enzymatic degradation of bovine serum Albumin nanoparticles for drug delivery.
- 101 p.
Source: Masters Abstracts International, Volume: 48-03, page: 1728.
Thesis (M.Sc.)--University of Alberta (Canada), 2010.
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, zetapotential, 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.
ISBN: 9780494559598Subjects--Topical Terms:
550957
Chemistry, Pharmaceutical.
Enzymatic degradation of bovine serum Albumin nanoparticles for drug delivery.
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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, zetapotential, 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.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR55959
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