کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8994356 | 1114394 | 2005 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Uniform Encapsulation of Stable Protein Nanoparticles Produced by Spray Freezing for the Reduction of Burst Release
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کلمات کلیدی
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
اکتشاف دارویی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Uniform Encapsulation of Stable Protein Nanoparticles Produced by Spray Freezing for the Reduction of Burst Release Uniform Encapsulation of Stable Protein Nanoparticles Produced by Spray Freezing for the Reduction of Burst Release](/preview/png/8994356.png)
چکیده انگلیسی
Stable protein nanostructured particles, produced by spray freezing into liquid (SFL) nitrogen, were encapsulated uniformly into microspheres to reduce the burst release over the first 24 h. The denaturation and aggregation of these bovine serum albumin (BSA) highâsurface area particles were minimal due to ultraârapid freezing and the absence of a liquid-air interface. Upon sonication, these friable highly porous, solid protein particle aggregates broke up into submicron particles. These particles were encapsulated into DLâlactide/glycolide copolymer (PLGA) and poly(lactic acid) (PLA) microspheres by anhydrous solidâinâoilâinâoil (s/o/o) techniques. For 5% loading of protein, the burst release after 24 h was only 2.5-4.1%, that is, values fivefold to tenfold lower than those observed for larger more conventional BSA particles. At a loading of 10%, the burst was only 6 and 13% for PLGA and PLA, respectively, and at 15% loading it was only 12% for PLGA. As shown with confocal and scanning electron microscopy (SEM), the low burst is consistent with a uniform distribution of protein nanoparticles, which were about 100 times smaller than the microspheres. Changes in aggregation and secondary structure, which were monitored by size exclusion chromatography and FTIR, respectively, indicated only slight monomer loss (3.9%) and high structural integrity (38% αâhelix) in the encapsulated protein. © 2004 WileyâLiss, Inc. and the American Pharmacists Association J Pharm Sci 94:56-69, 2005
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Pharmaceutical Sciences - Volume 94, Issue 1, January 2005, Pages 56-69
Journal: Journal of Pharmaceutical Sciences - Volume 94, Issue 1, January 2005, Pages 56-69
نویسندگان
W.Thomas Leach, Dale T. Simpson, Tibisay N. Val, Efemona C. Anuta, Zhongshui Yu, Robert O. III, Keith P. Johnston,