کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7693799 | 1496467 | 2018 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Engineered protein scaffolds as leads for synthetic inhibitors of protein-protein interactions
ترجمه فارسی عنوان
داربست های پروتئینی مهندسی شده به عنوان منبعی برای مهارکننده های متقابل پروتئین و پروتئین منجر شده اند
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موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی (عمومی)
چکیده انگلیسی
Rationally designed protein-protein interaction inhibitors mimic interfacial binding epitopes, specifically residues that contribute significantly to binding. However, direct mimicry often does not lead to high affinity ligands because the natural complexes themselves are functionally transient and of low affinity. The mimics typically need to be optimized for potency. Engineered proteins displaying conformationally-defined epitopes may serve as attractive alternatives to natural protein partners as they can be strictly screened for tight binding. The advantage of focused screens with conformationally-defined protein scaffolds is that conservation of the geometry of the natural binding epitopes may preserve binding site specificity while allowing direct mimicry by various synthetic secondary structure scaffolds. Here we review different classes of engineered proteins for their binding epitope geometry and as leads for synthetic secondary and tertiary structure mimics.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Current Opinion in Chemical Biology - Volume 44, June 2018, Pages 16-22
Journal: Current Opinion in Chemical Biology - Volume 44, June 2018, Pages 16-22
نویسندگان
Michael G Wuo, Paramjit S Arora,