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Crystal structures of amyloidogenic segments of human transthyretin.

Protein Sci.. 2018-07; 
SaelicesLorena,SieversStuart A,SawayaMichael R,EisenbergDav
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Peptide Synthesis … This article is protected by copyright. All rights reserved. Page 12. 12 Material and Methods Sample preparation and crystallization conditions. Peptides were synthesized at > 97% purity from GenScript (Piscataway, NJ, USA) and GL Biochem (Shanghai) Ltd. (Shanghai, China) … Get A Quote

摘要

Amyloid diseases are characterized by the deposition of proteins in the form of amyloid fibrils, in organs that eventually fail. The development of effective drug candidates follows from the understanding of the molecular processes that lead to protein aggregation. Here, we study amyloidogenic segments of transthyretin (TTR). TTR is a transporter of thyroxine and retinol in the blood and cerebrospinal fluid. When mutated and/or as a result of aging, TTR aggregates into amyloid fibrils that accumulate in organs such as the heart. Recently, we reported two amyloidogenic segments that drive amyloid aggregation. Here, we report the crystal structure of another six amyloidogenic segments of TTR. We found t... More

关键词

amyloid,amyloidogenic segments,crystallography,out-of-register,steric zipper,transthyr
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