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- W2804244900 abstract "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." @default.
- W2804244900 created "2018-06-01" @default.
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- W2804244900 date "2018-06-01" @default.
- W2804244900 modified "2023-10-17" @default.
- W2804244900 title "Engineered protein scaffolds as leads for synthetic inhibitors of protein–protein interactions" @default.
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- W2804244900 doi "https://doi.org/10.1016/j.cbpa.2018.05.013" @default.
- W2804244900 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5967659" @default.
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