Structural stability of transthyretin in acidic conditions
نویسندگان
چکیده
منابع مشابه
The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions.
The L55P transthyretin (TTR) familial amyloid polyneuropathy-associated variant is distinct from the other TTR variants studied to date and the wild-type protein in that the L55P tetramer can dissociate to the monomeric amyloidogenic intermediate and form fibril precursors under physiological conditions (pH 7.0, 37 degrees C). The activation barrier associated with L55P-TTR tetramer dissociatio...
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A stability indicating High-Performance Liquid Chromatography (HPLC) method wasvalidated and used to study the degradation of cetirizine dihydrochloride in acidic and oxidativeconditions. The separation was carried out on a Symmetry C18 column and a mixture of 50 mMKH2PO4 and acetonitrile (60:40 v/v, pH = 3.5) was used as the mobile phase. The method waslinear over the range of 1-20 μg/mL of ce...
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A stability indicating High-Performance Liquid Chromatography (HPLC) method wasvalidated and used to study the degradation of cetirizine dihydrochloride in acidic and oxidativeconditions. The separation was carried out on a Symmetry C18 column and a mixture of 50 mMKH2PO4 and acetonitrile (60:40 v/v, pH = 3.5) was used as the mobile phase. The method waslinear over the range of 1-20 μg/mL of ce...
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متن کاملQuantification of Quaternary Structure Stability in Aggregation-Prone Proteins under Physiological Conditions: The Transthyretin Case
The quaternary structure stability of proteins is typically studied under conditions that accelerate their aggregation/unfolding processes on convenient laboratory time scales. Such conditions include high temperature or pressure, chaotrope-mediated unfolding, or low or high pH. These approaches have the limitation of being nonphysiological and that the concentration of the protein in solution ...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2003
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.43.s64_3