کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9918579 | 1557549 | 2005 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Effect of lyophilization on the structure and phase changes of PEGylated-bovine serum albumin
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
علوم دارویی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Poly (ethylene glycol) (PEG) conjugation masks the protein's surface and increases the molecular size of the polypeptide, thus preventing the approach of antibodies or antigen processing cells and reducing the degradation by proteolytic enzymes. Proteins are readily denatured by numerous stresses arising in solution (e.g., heating, agitation, freezing and pH changes) or by chemical reactions (e.g., hydrolysis and deamidation), many of which are mediated by water. Lyophilization is most commonly used to prepare dehydrated proteins, which, theoretically, should have the desired long-term stability at ambient temperatures. Through Raman spectroscopy, differential scanning calorimetry (DSC) associated with the determination of water content by Karl Fisher titration, it was observed that after the modification of BSA-PEG in a ratio of 1:0.25 showed lower degree of structural alterations and consequently lower variation on the physical-chemical characteristics when it was compared to BSA-PEG (1:0.5). Moreover, the BSA-PEG (1:0.25) optimizes the conditions during the lyophilization process and storage of the protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Pharmaceutics - Volume 304, Issues 1â2, 4 November 2005, Pages 124-134
Journal: International Journal of Pharmaceutics - Volume 304, Issues 1â2, 4 November 2005, Pages 124-134
نویسندگان
Virgilio Jr., Duclerc F. Parra, Bronislaw Polakiewicz, Ronaldo N.M. Pitombo,