A capillary electrophoretic–mass spectrometric method for the assessment of octreotide stability under stress conditions

A capillary electrophoretic–mass spectrometric method for the assessment of octreotide stability under stress conditions


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پژوهان
صفحه نخست سامانه
چکیده مقاله
چکیده مقاله
نویسندگان
نویسندگان
دانلود مقاله
دانلود مقاله
دانشگاه علوم پزشکی تبریز
دانشگاه علوم پزشکی تبریز

نویسندگان: ال ناز تمیزی , ابوالقاسم جویبان

کلمات کلیدی:

نشریه: 19680 , 1429 , - , 2016

اطلاعات کلی مقاله
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نویسنده ثبت کننده مقاله ال ناز تمیزی
مرحله جاری مقاله تایید نهایی
دانشکده/مرکز مربوطه مرکز تحقیقات کاربردی دارویی
کد مقاله 61368
عنوان فارسی مقاله A capillary electrophoretic–mass spectrometric method for the assessment of octreotide stability under stress conditions
عنوان لاتین مقاله A capillary electrophoretic–mass spectrometric method for the assessment of octreotide stability under stress conditions
ناشر 6
آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ بلی
عنوان نشریه (خارج از لیست فوق)
نوع مقاله Original Article
نحوه ایندکس شدن مقاله ایندکس شده سطح یک – ISI - Web of Science
آدرس لینک مقاله/ همایش در شبکه اینترنت http://www.sciencedirect.com/science/article/pii/S0021967315018348?via%3Dihub

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A capillary zone electrophoretic-electrospray ion trap mass spectrometric method has been developed to assess the stability and pathways of degradation of the cancer therapeutic octapeptide, octreotide. As a somatostatin analogue, octreotide contains a single disulphide bond linking Cys2–Cys7 of NH2-D-Phe-Cys-Phe-D-Trp-Lys-Thr-Cys-The-OH . Resolution of octreotide from its degradation products was achieved using a capillary zone electrophoretic method with bare fused silica capillaries, a 10 mM ammonium formate buffer, pH 3.20, at 25 C and an applied voltage of 25 kV. An ion trap low energy collision induced dissociation procedure was applied for the characterization of the chemical structures of the degradation products derived from an acidic, alkaline, neutral and thermal solution treatment of octreotide. The results so obtained indicated that linear octreotide degradation products were formed under acidic and alkaline conditions, due to the hydrolysis of a ring amide bond and a hitherto unknown desulfurization of the Cys–Cys disulfide bond, respectively. Degradation under neutral conditions occurred via cleavage of the exocyclic N-((2R,3R)-1,3-dihydroxybutan-2-yl) amide bond which also preceded the ring amide hydrolysis under acidic conditions. The developed method was further successfully applied to assess the kinetics of these octreotide degradations. Overall, this method is suitable for the rapid and precise assessment of the stability and quality control of octreotide as a synthetic peptide-based pharmaceutical product, and has led to the discovery of a new Cys–Cys disulfide degradation pathway.

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نویسنده نفر چندم مقاله
ال ناز تمیزیاول
ابوالقاسم جویبانسوم

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نام فایل تاریخ درج فایل اندازه فایل دانلود
Journal of Chromatography A 1429, 354-363, 2016.pdf1396/06/161328590دانلود