کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10613301 | 986879 | 2005 | 15 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The influence of protein solubilisation, conformation and size on the burst release from poly(lactide-co-glycolide) microspheres
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی مواد
بیومتریال
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: The influence of protein solubilisation, conformation and size on the burst release from poly(lactide-co-glycolide) microspheres The influence of protein solubilisation, conformation and size on the burst release from poly(lactide-co-glycolide) microspheres](/preview/png/10613301.png)
چکیده انگلیسی
Encapsulation of proteins in poly(lactide-co-glycolide) microspheres via emulsion is known to cause insoluble protein aggregates. Following protein emulsification and encapsulation in PLGA microspheres, we used circular dichroism to show that the recoverable soluble protein fraction also suffers subtle conformational changes. For a panel of proteins selected on the basis of molecular size and structural class, conformational stability measured by chemical denaturation was not indicative of stability during emulsion-encapsulation. Partial loss of structure was observed for α-helical proteins released from freeze-dried microspheres in aqueous buffer, with dramatic loss of structure for a β-sandwich protein. The addition of sucrose (a lyoprotectant) did not prevent the loss of protein conformation upon encapsulation. Therefore, the conformational changes seen for the released soluble protein fraction originates during emulsification rather than microsphere freeze-drying. Analysis of the burst release for all proteins in buffer containing denaturant or surfactant showed that the degree of protein solubilisation was the dominant factor in determining the initial rate and extent of release. Our data for protein release into increasing concentrations of denaturing buffer suggest that the emulsion-denatured protein fraction remains insoluble; this fraction may represent the protein loss encountered upon comparison of protein encapsulated versus protein released.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Controlled Release - Volume 110, Issue 1, 10 December 2005, Pages 34-48
Journal: Journal of Controlled Release - Volume 110, Issue 1, 10 December 2005, Pages 34-48
نویسندگان
Gayle Duncan, Thomas J. Jess, Farahidah Mohamed, Nicholas C. Price, Sharon M. Kelly, Christopher F. van der Walle,