Expression and purification of a recombinant amyloidogenic peptide from transthyretin for solid-state NMR spectroscopy

被引：4

作者：

Nadaud, Philippe S. ^{[1
]}

Sarkar, Mohosin ^{[1
]}

Wu, Bo ^{[1
]}

MacPhee, Cait E. ^{[2
]}

Magliery, Thomas J. ^{[1
,3
]}

Jaroniec, Christopher P. ^{[1
]}

机构：

[1] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA

[2] Univ Edinburgh, SUPA, Sch Phys & Astron, Edinburgh EH9 3JZ, Midlothian, Scotland

[3] Ohio State Univ, Dept Biochem, Columbus, OH 43210 USA

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2010年 / 70卷 / 01期

基金：

美国国家科学基金会; 英国生物技术与生命科学研究理事会;

关键词：

Fusion protein; GB1; Recombinant human transthyretin 105-115; Escherichia coli BL21(DE3); Ni2+ affinity chromatography; Amyloid fibrils; Solid-state NMR spectroscopy; ALPHA-SYNUCLEIN FIBRILS; BETA-SHEET STRUCTURE; HUMAN PRION PROTEIN; ANGLE-SPINNING NMR; ESCHERICHIA-COLI; HIGH-RESOLUTION; MOLECULAR-CONFORMATION; STRUCTURAL MODEL; RESIDUES; SYSTEM;

D O I：

10.1016/j.pep.2009.09.017

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

We describe the expression and purification of a model amyloidogenic peptide comprising residues 105-115 of human transthyretin (TTR105-115). Recombinant TTR105-115, which does not contain any non-native residues, was prepared as part of a fusion protein construct with a highly soluble B1 immunoglobulin binding domain of protein G (GB1), with typical yields of similar to 4 mg/L of uniformly C-13,N-15-enriched HPLC-purified peptide per liter of minimal media culture. Amyloid fibrils formed by recombinant TTR105-115 were characterized by transmission electron microscopy and solid-state NMR spectroscopy, and found to be comparable to synthetic TTR105-115 fibrils. These results establish recombinant TTR105-115 as a valuable model system for the development of new solid-state NMR techniques for the atomic-level characterization of amyloid architecture. (C) 2009 Elsevier Inc. All rights reserved.

引用

页码：101 / 108

页数：8

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