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Article

Design of amyloidogenic peptide traps

2023-01-13

Abstract excerpt

Segments of proteins with β-strand propensity can self associate to form amyloid fibrils associated with many diseases. These regions often adopt alternative structures in their folded states, or are intrinsically disordered in solution, making it difficult to generate binders or inhibitors with existing strategies. Here we describe a general approach to bind such segments in β-strand and β-hairpin conformations u...

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Identifiers and source

Literature Corpus work
bbbc2135-e455-5c70-bf25-ee4c0c187182
DOI
10.1101/2023.01.13.523785
Open publication

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Design of amyloidogenic peptide trapsDOI 10.1101/2023.01.13.523785
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