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A peptide from the adenovirus fiber shaft forms amyloid‐type fibrils
[摘要]

The fiber protein of adenovirus consists of a C-terminal globular head, a shaft and a short N-terminal tail. The crystal structure of a stable domain comprising the head plus a part of the shaft of human adenovirus type 2 fiber has recently been solved at 2.4 Å resolution [van Raaij et al. (1999) Nature 401, 935–938]. A peptide corresponding to the portion of the shaft immediately adjacent to the head (residues 355–396) has been synthesized chemically. The peptide failed to assemble correctly and instead formed amyloid-type fibrils as assessed by electron microscopy, Congo red binding and X-ray diffraction. Peptides corresponding to the fiber shaft could provide a model system to study mechanisms of amyloid fibril formation.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] Adenovirus;Amyloid fibril;Electron microscopy;Congo red;X-ray diffraction;Boc;tert-butyloxycarbonyl;HPLC;high performance liquid chromatography;GdnHCl;guanidine hydrochloride;HAd2;human adenovirus serotype 2;SDS;sodium dodecyl sulfate [时效性] 
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