کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10235640 45050 2011 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Exploring possibility of promiscuity of amyloid inhibitor: Studies on effect of selected compounds on folding and amyloid formation of proteins
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Exploring possibility of promiscuity of amyloid inhibitor: Studies on effect of selected compounds on folding and amyloid formation of proteins
چکیده انگلیسی
Fibrillar protein aggregates called amyloids are the hallmark of several degenerative diseases. Identification of common drugs which are capable of blocking or inhibiting protein aggregation may be considered as one of the therapeutic approaches directed against amyloid diseases. The present study describes the effect of a few small molecule compounds like clotrimazole, sulconazole and rottlerin towards amyloidogenesis of two model proteins unrelated in terms of structure and sequence such as hen egg white lysozyme and cytochrome c to test promiscuity of amyloid inhibition. Amyloid progression was monitored through Thioflavin T assay and atomic force microscope imaging. Also, the thermodynamic basis of inhibition of fibrillogenesis was analyzed through equilibrium unfolding and unfolding kinetic studies of the proteins in presence of the compounds. Structural alterations in the aggregation-prone intermediate state conformation of the protein in presence of the compounds were monitored through 1-anilino-8-naphthalene sulfonate (ANS) binding studies. Our findings shed some light on the key interactions that guide the path towards protein aggregation and the probable structural and thermodynamic mechanism of inhibition which may provide useful guidelines in development of therapeutics against amyloid diseases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Process Biochemistry - Volume 46, Issue 5, May 2011, Pages 1179-1185
نویسندگان
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