کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5511829 1540215 2017 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Research ArticleMechanistic insight into interaction of Sodium Dodecyl Sulphate to asialylated form of glycoprotein: A mimic of membrane protein-lipid system
ترجمه فارسی عنوان
تحقیقات مقدمه ای از تعامل سدیم دودهیل سولفات با فرم اسیدیالیتی گلیکوپروتئین: یک نمونه از پروتئین-پروتئین غشائی
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
چکیده انگلیسی

The SDS-glycoprotein system is mimic of membrane protein-lipid system. Fate of glycoprotein, conformation and the interactive forces involved in membrane milieu are expected to be decided by the net charge on glycoprotein that may change during acidic environment in a range of pathological states, including cancer, stroke, and ischemia. Asialofetuin (ASF; asialylated form of glycoprotein) and SDS interaction is studied when glycoprotein bears varying range of net charge (i.e. at different pH's) by steady state and time-resolved spectroscopic, calorimetric and microscopic approaches. SDS interacts differently with ASF when protein is in cationic (at pH 2, 3 and 4) and in anionic states (pH 7.4). ASF undergo aggregation at pH 2, 3 and 4 whereas have enhancement in α-helical structure at pH 7.4 at sub-micellar concentrations of SDS. At pH 2, 3 and 4, the positively charged ASF interacts electrostatically with negatively charged head groups of SDS, leaving its hydrophobic tail free to interact with other protein-SDS complex and consequently lead to amyloid formation. However, at pH 7.4, the ASF interacts hydrophobically with SDS and an increase in α-helical content occurs that constrains the environment of Trp51 and consequently decreases movement of Trp conformers.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 103, October 2017, Pages 65-73
نویسندگان
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